2016-2017 report - labos ulglabos.ulg.ac.be/.../sites/19/2016/06/ra2016-2017-1.pdf · academy of...

2016-2017 REPORT

CONTENTS INTRODUCTION 3

RESEARCH GROUPS 5

EXPERTISE 7 MAJOR EQUIPMENT 9 HIGHLIGHTS OF THE YEAR 12 SCIENTIFIC SERVICES 29 SCIENTIFIC PRODUCTION 34 - Awards 34 - Invited speakers 35 - Oral presentations 36 - PhD theses 40 - Publications 41 - Symposia 50 EDUCATION 52 - Academic courses 52 - Trainees and students 56 - General public activities 61 - Wide audience conferences 62 NATIONAL & INTERNATIONAL EXCHANGES 63 - Postdocs In 63 - Collaborations 66 - Stays in other institutions 74 - Visitors 75 FUNDING 76

MISSIONS OF EXPERTISE 80 COMMITTEES AND SOCIETIES 82 COMPOSITION OF THE CENTER 84

INTRODUCTION

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The Centre of Protein Engineering or CIP is part of the Faculty of Sciences of the University of Liège. Its research activities are carried out within the InBioS (Integrative Biological Sciences) Research Unit and it is involved in the teaching program of the Department of Life Sciences. Since its creation, the vocation of the CIP has been the study and the analysis of the proteins from the isolated molecules, their structure and function, to their integrations in complex cellular networks. To reach these goals, the members of the CIP have continually tried to implement the most innovative experimental approaches and techniques. These are constantly improved within the different groups that have been created. In recent years, 9 groups, working in close collaboration, have carried out numerous research projects and participated in European, federal, regional, French community and institutional projects. To support its research, the CIP has developed two technological platforms that constitute bridges between fundamental and applied research between the academic world and private sector. Protein Factory (http://www.proteinfactory.ulg.ac.be/) and Robotein (http://www.robotein.ulg.ac.be/) have requested their positioning as CAREs within the University of Liège. More information on the CIP and the two CAREs can be found on the recently updated CIP website (http://labos.ulg.ac.be/cip/). The Centre is involved in a large number of national and international collaborations and has hosted three foreign postdocs including Dr Mareike Jakobs and Dr Ruth Kellner from Germany and Dr Anna Wiktoria Wypijewska del Nogal from Poland. The year 2016 was marked by the retirement of Dr Colette Duez, a FNRS Research Associate who almost spent her complete career in the CIP. She left us in October 2016. Her knowledge of bacterial genetics has always been a reference for the entire group. In the same way, her commitment and her rigor in the day-to-day supervision of all the researchers, in particular beginners, must be underlined. Colette also participated, as secretary, in the management of the F.R.S.-FNRS "Belgium Interdisciplinary Biofilm Research" contact group. We sincerely thank her for her major contributions to the activities of the Centre during all these years and we wish her the best for years to come. We also wish to underline the accomplishments of three other CIP members: Professor André Matagne had the honor of being elected titular member of the Belgian Royal

Academy of Sciences in February 27, 2016. Dr Annick Wilmotte has been nominated as a Belgian Woman Scientist to participate in the

Wikibomb organized by the Scientific Committee on Antarctic Research (SCAR). In October 2017, Dr Sébastien Rigali has been promoted “Maître de Recherche” at the FNRS. By browsing these pages, you will discover the scientific results accumulated over the last two years, in particular in the form of highlights. In summary, during this period, the CIP members produced a total of 51 publications, 11 PhD theses and organized 14 national and international meetings. We want to take advantage of this opportunity to thank and congratulate all the CIP members who participated in the many research and teaching tasks and hope that you will enjoy reading this report.

Paulette Charlier

RESEARCH GROUPS

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BACTERIAL DIVERSITY, PHYSIOLOGY AND GENETICS

Group leader Prof. Bernard Joris Permanent scientists Dr Colette Duez

Dr Colette Goffin

Dr Mohammed Terrak

Dr Annick Wilmotte

Associate members Dr Ana Amoroso

Dr Fabien Borderie

Mme Charlotte Crahay

Dr Michaël Delmarcelle

Dr Yannick Lara

Dr Serge Leimanis

Dr Samir Olatunji

Mr Patrick Stefanic

Mr Olivier Verlaine

BIOLOGICAL MACROMOLECULES AND BIOCHEMISTRY

Group leader Prof. Moreno Galleni Permanent scientists Dr Georges Feller

Dr Sébastien Rigali

Associate members Dr Ahlem Bouaziz

Dr Paola Mercuri

Dr Caroline Montagner

Dr Elodie Tenconi

Dr Marylène Vandevenne

BIOLOGICAL MACROMOLECULE CRYSTALLOGRAPHY AND MODELING

Group leader Prof. Paulette Charlier Permanent scientist Dr Frédéric Kerff

Associate members Dr Eric Sauvage

Dr Meriem El Ghachi

RESEARCH GROUPS

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ENZYMOLOGY AND PROTEIN FOLDING

Group leader Prof. André Matagne Permanent scientist Dr Mireille Dumoulin

Associate members Dr Kishore Babu Bobbili

Dr Julie Vandenameele

Dr Ruth Kellner

EXPERTISE

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MOLECULAR BIOLOGY Activity screening Gene cloning in Escherichia. coli, Bacillus, Streptomyces and Pichia pastoris Site-directed mutagenesis Phage display High-throughput amplicon sequencing and metagenomics Genome sequencing, assembly and annotation Protein engineering (random mutagenesis, protein design)

PROTEIN PRODUCTION

In Escherichia coli, Bacillus, Streptomyces, Lactococcus lactis, Pichia pastoris or in

environmental strains From mL to 60 L In flasks or fermentors Optimisation of industrial processes

2H, 13C, 15N enrichment for NMR studies Selenomethionine enrichment for crystallography studies

PROTEIN PURIFICATION

Purification of soluble and membrane proteins Classical purification techniques (ion exchange, affinity, hydroxyapatite…) From mg to g HPLC, FPLC, Åkta prime, Åkta explorer, Profinia, Biopilot…

MACROMOLECULE CHARACTERISATION

Biochemical characterisation

Cellular localization of proteins: o Fluorescence microscopy

2D-DIGE DDGE ELISA EMSA Enzymology:

o Steady and transient states kinetics o Stopped-flow & quenched-flow

N-terminal sequencing Protein-protein interactions:

o Bacterial two hybrids and immunoprecipitation Proteomics Western blot

EXPERTISE

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Biophysical characterization Microcalorimetry (DSC and ITC) Bio-layer interferometry (Octet HTX) Dynamic/static light scattering Analysis of peptidoglycan by HPLC Protein stability, folding and aggregation:

o Spectroscopy: UV-Vis, fluorescence and circular dichroism o Time-resolved spectroscopy o Hydrogen-deuterium exchange

X-Ray crystallography: o Crystallogenesis o de novo structure determination o Studies of ligand-protein complexes o 3D structure determination

IN SILICO STUDIES Phylogenetic analyses Prokaryotic regulon predictions: web tool PREDetector (Prokaryotic Regulatory Elements

Detector)

MAJOR EQUIPMENT

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GENETIC ENGINEERING AND MOLECULAR BIOLOGY

1 Gene Pulser electroporator (Biorad) Several PCR apparatus including: 1 MJ Mini Real Time Quantitative PCR PTC0148 (Biorad) 1 Nanovue (GE Healthcare)

ALGAL CULTURES

1 Versatile environment test chamber (Sanyo) 3 Light thermostatized incubators (LMS)

MICROBIAL CULTURES

2 Controlled environment incubator shakers (New Brunswick Scientific) 11 Incubator shakers: five G-25 (New Brunswick Scientific), one 25D (New Brunswick Scientific), one Excella E24 (New Brunswick Scientific), two Innova 44 (New Brunswick Scientific) and two Innova 4330 (New Brunswick Scientific) 1 Gradient table for crossed gradients of temperature and light (Labio chromatography) 1 Thermomixer C Eppendorf

PROTEIN PRODUCTION

Five fermentors including: one 5 L (Biostat, B. Braun Biotech International), one 10 L (Bioflow 3000, New Brunswick scientific), two 20 L (Bioflow 4500, New Brunswick scientific) and one 80 L (Bioflow 5000, New Brunswick scientific). 1 Turbidimeter FSC402 (Mettler Toledo) 1 Steam generator Maxi 24 (Ghidini Benvenuto) 1 Colony Picker Microlab Starlet robot (Hamilton) with Hepa Filter

PROTEIN PURIFICATION

1 Continuous centrifugation system (SA 1-02-175 model, Westfalia) 2 homogenizers: one Panda (GEA Process Technology) and one Emulsiflex-C3 (Avestin, Inc) 3 sonicators: one MSE, one Sonifer B-12 (Branson Sonic Power Company) and one Bioruptor Plus (Diagenode). A range of instruments to perform protein purification at low or high pressure The most remarkable include: 2 Åkta-explorer (10S 2D-LC and 100-Air), 1 Åkta- purifier, 1 Åkta prime, 2 Åkta prime plus (GE Healthcare) and 3 NGC Bio-Rad 2 LC210 purification systems (Isco) 1 Microlab Star robot (Hamilton) 2 Profinia purification systems (Bio-Rad) 1 Tangential filtration system (Sartoflow Alpha, Sartorius) 1 Table top ultracentrifuge model OPTIMA MAX XP equipped with TLA-100, MLA-55 and MLA-55 rotors 1 Ultracentrifuge Optima XL-80K (Beckman)

MAJOR EQUIPMENT

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ANALYTICAL STUDIES

1 Circular Dichroism spectrophotometer J-810 equipped with a Peltier and a 6 cell holder (Jasco) 2 2D-electrophoresis GE Ettan IPGphor3 and Ettan DALTsix apparatus (GE Healthcare) 2 DGGE electrophoresis apparatus (Dcode, Biorad) 1 DynaPro NanoStar DLS/SLS recorder for Dynamic/Static Light Scattering (Wyatt Technology Corporation) 3 Fluorimeters: FP-8300 (Jasco), Carry Eclipse (Varian) and LS50B (Perkin-Elmer) 1 HPLC Alliance with an auto-injection system equipped with 3 detector modes: UV/vis (diode array), fluorescence and refractometer and a fraction collector (Waters) 2 Microcalorimeters: ITC200 (isothermal titration calorimetry) and VP-DSC (differential scanning calorimetry) from GE-MicroCal 5 Microplate readers: one Labsystems Multiskan Multisoft (TechGen International), one PowerwaveX (Bio-Tek instruments, Inc), one Tecan Infinite 200 PRO UV/Vis + fluorescence, one Tecan Infinite 200 PRO UV/Vis + chemiluminescence with injectors, one Spectra Max M2 Molecular Devices (fluorescence and absorbance). 1 Microplate Strip Washer EL X 50 (Bio-Tek Instruments, Inc) 1 Procise 492 N-terminus amino acid sequencer (Applied Biosystems, Perkin Elmer) 1 Quenched-flow SFM 400 (Bio-Logic) 1 Rapid filtration system (Bio-Logic) Several spectrophotometers: Uvikon (Bio-Tek Instruments, Inc,), Carry 100 Biomelt (Varian), Specord 50 and 200 (Analytik Jena), V-630 (Jasco) 1 Stopped-flow apparatus: SFM300 combined with MOS450 for UV/visible light, fluorescence and circular dichroism detection 1 Fortebio Octet HTX (Pall) 1 Labchip GXII (Perkin Elmer) 1 SEC-MALS (size exclusion chromatography-multiangle light scattering) miniDAWN TREOS II AQUEOUS (Wyatt) coupled with a HPLC BIOinert LC20Ai (Shimadzu) with RID-20A, SIL-20AC Autosampler and SPD-20A UV-Vis detector (Shimadzu)

CRYSTALLOGRAPHY

1 Cryogenic AD41 cryosystem (Oxford) 4 Graphic-PC stations (Linux) 1 Imaging Plate Marresearch IPmar345 with an Incoatec IµS X-ray microfocus source (Rigaku) 1 Minstrel DT Imager: crystal imaging and protein crystal monitoring systems (Rigaku) 1 TTP Labtech Mosquito Crystallization robot (compact bench-top instrument for nanolitre liquid handling) (Cambridge UK)

IMAGING

1 Axio Imager Z1 fluorescent microscope (Zeiss) 1 camera for digitalisation of images and analytical analyses (Olympus) 1 CKX 31 inversed microscope (Olympus) 1 BX43 microscope (Olympus) 1 DMLB2 microscope (Leica) 1 Molecular Imager FX system (Biorad) 1 Phase contrast microscope (Reichert) 1 binocular microscope (model SZ-6 PHOTO Bauch & Lomb) 1 binocular microscope with a digital camera (SMZ1500, Nikon)

MAJOR EQUIPMENT

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1 microscope equipped for epifluorescence (Zeiss) 1 stereomicroscope Stemi 2000C, 10*/23 BR FOC ocular (Zeiss) 1 Typhoon Trio + scanner (GE Healthcare) 1 LAS 4000 camera (GE Healthcare)

MICROFLUIDIC PLATFORM

1 Microfluidic pump system (model MFCS-Flex Fluidgen) 1 Industrial camera (National instrument) 1 Labview station for real-time control and monitoring (National instrument) 2 Low pulse flow peristaltic pumps (Ismatec) 1 8-channel peristaltic pump (model 205C Watson Marlow) 1 Fastgene LED Transilluminator (Nippon Genetics)

MISCELLANEOUS

1 Freeze-dryer (Christ)

HIGHLIGHTS OF THE YEAR

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A Phenotypic and Genotypic Analysis of the Antimicrobial Potential of

Cultivable Streptomyces Isolated from Cave Moonmilk Deposits. Maciejewska M†, Adam D†, Martinet L, Naômé A, Całusińska M, Delfosse P, Carnol M, Barton HA, Hayette MP, Smargiasso N, De Pauw E, Hanikenne M, Baurain D, Rigali S. † These authors contributed equally to this work. Front Microbiol. 7:1455. eCollection 2016; doi:10.3389/fmicb.2016.01455, 2016 Moonmilk speleothems of limestone caves host a rich microbiome, among which Actinobacteria represent one of the most abundant phyla. Ancient medical texts reported that moonmilk had therapeutical properties, thereby suggesting that its filamentous endemic actinobacterial population might be a source of natural products useful in human treatment. In this work, a screening approach was undertaken in order to isolate cultivable Actinobacteria from moonmilk of the Grotte des Collemboles in Belgium, to evaluate their taxonomic profile, and to assess their potential in biosynthesis of antimicrobials. Phylotype representatives were tested for antibacterial and antifungal activities and their genomes were mined for secondary metabolite biosynthetic genes coding for non-ribosomal peptide synthetases (NRPSs), and polyketide synthases (PKS). The moonmilk Streptomyces collection was found to display strong inhibitory activities against a wide range of reference organisms, as 94, 71, and 94% of the isolates inhibited or impaired the growth of Gram-positive, Gram-negative bacteria, and fungi, respectively. Interestingly, 90% of the cave strains induced strong growth suppression against the multi-drug resistant Rasamsonia

argillacea, a causative agent of invasive mycosis in cystic fibrosis and chronic granulomatous diseases. Overall, our work supports the common belief that moonmilk might effectively treat various infectious diseases thanks to the presence of a highly diverse population of prolific antimicrobial producing Streptomyces, and thus may indeed constitute a promising reservoir of potentially novel active natural compounds.

The global antimicrobial

pattern of moonmilk

Streptomyces isolates and

their presumed secondary

metabolites biosynthesis

potential based on genome mining. The heatmap plot, correlated with MLSA-based phylogeny, represents the mean of the antifungal and antibacterial (Gram-positive and Gram-negative bacteria) activities for each of the 30 phylotype representatives (MM strains), together with the sum of those activities. In addition, the greyscale on the heatmap displays the

biosynthetic genes content of individual strain, including number of its NRPS, PKS-I, PKS-II, and PKS-III genes, together with their total number.


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The CebE/MsiK Transporter is a Doorway to the Cello-oligosaccharide-

mediated Induction of Streptomyces scabies Pathogenicity. Jourdan S†, Francis IM†, Kim MJ, Salazar JJ, Planckaert S, Frère JM, Matagne A, Kerff F, Devreese B, Loria R, Rigali S. †These authors contributed equally to this work. Sci Rep. 6:27144; doi: 10.1038/srep27144, 2016

Streptomyces scabies is an economically important plant pathogen well-known for damaging root and tuber crops by causing scab lesions. Thaxtomin A is the main causative agent responsible for the pathogenicity of S. scabies and cello-oligosaccharides are environmental triggers that induce the production of this phytotoxin. How cello-oligosaccharides are sensed or transported in order to induce the virulent behavior of S. scabies? Here we report that the cellobiose and cellotriose binding protein CebE, and MsiK, the ATPase providing energy for carbohydrates transport, are the protagonists of the cello-oligosaccharide mediated induction of thaxtomin production in S. scabies. Our work provides the first example where the transport and not the sensing of major constituents of the plant host is the central mechanism associated with virulence of the pathogen. Our results allow to draw a complete pathway from signal transport to phytotoxin production where each step of the cascade is controlled by CebR, the cellulose utilization regulator. We propose the high affinity of CebE to cellotriose as possible adaptation of S. scabies to colonize expanding plant tissue. Our work further

highlights how genes associated with primary metabolism in nonpathogenic Streptomyces species have been recruited as basic elements of virulence in plant pathogenic species.

Model of the cellobiose/cellotriose-

mediated induction of thaxtomin production in S. scabies. In this work we show that the cello-oligosaccharide-induced pathogenicity of S. scabies 87–22 is mediated, at least in great part, through the CebEFG-MsiK ABC transporter system. This allows to propose a first signaling pathway from cello-oligosaccharide transport to the production of thaxtomin A (txt genes) in S. scabies, with each step of the cascade controlled by the cellulose utilization transcriptional repressor CebR


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Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein

localized at the division site

Maréchal M, Amoroso A, Morlot C, Vernet T, Coyette J, Joris B. BMC Microbiol. 12;16(1):239 doi:10.1186/s12866-016-0844-y, 2016

Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, is now renamed LcpA. Previously, it was associated with the regulation of the expression of the low-affinity PBP5 and -lactam resistance and also been involved in the regulation of several additional surface-related properties, including increased sensitivity to lysozyme, increased rate of cellular autolysis and decrease of the rhamnose amount in the cell wall. In this study, the LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae. LcpA belongs to the LytR-CpsA-Psr family. In conclusion to our work, its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, indicate that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.

A) LcpA immunolocalization in E. hirae cells. The upper panels show cells at an early division stage, the lower panels show cells at a later stage of division. B) PBP5 immunolocalization in E. hirae cells. The upper panels show cells at an early division stage, the lower panels show cells at a later stage of division. C)

Phylogeny analysis. Phylogenetic tree, based on the multiple alignment of LCP proteins from E. hirae, B.

subtilis and S. aureus, showing the relatedness of LCP proteins. D) Binding of LcpA to E. hirae cell wall.

Abbreviations: SCWP and (SCWP) stand for with or without secondary cell wall polymers.

A

B

C

D


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On the use of high-throughput sequencing for the study of cyanobacterial

diversity in Antarctic aquatic mats. Pessi IS, Maalouf P de C, Laughinghouse IV HD, Baurain D, Wilmotte A. J Phycol. 52:356–368, 2016. doi: 10.1111/jpy.12399 The study of Antarctic cyanobacterial diversity has been mostly limited to morphological identification and traditional molecular techniques. High- throughput sequencing (HTS) allows a much better understanding of microbial distribution in the environment, but its application is hampered by several methodological and analytical challenges. In this work, we explored the use of HTS as a tool for the study of cyanobacterial diversity in Antarctic aquatic microbial mats. Our results highlight the importance of using artificial communities to validate the parameters of the bioinformatics procedure used to analyze natural communities, since pipeline-dependent biases had a strong effect on the observed community structures. Analysis of microbial mats from five Antarctic lakes and an aquatic biofilm from the Sub-Antarctic showed that HTS is a valuable tool for the assessment of cyanobacterial diversity. The majority of the operational taxonomic units retrieved were related to filamentous taxa such as Leptolyngbya and Phormidium, which are common genera in Antarctic lacustrine microbial mats. However, other phylotypes related to different taxa such as Geitlerinema, Pseudanabaena, Synechococcus, Chamaesiphon, Calothrix, and Coleodesmium were also found. Results revealed a much higher diversity than what had been reported using traditional methods and also highlighted remarkable differences between the cyanobacterial communities of the studied lakes. The aquatic biofilm from the Sub-Antarctic had a distinct cyanobacterial community from the Antarctic lakes, which in turn displayed a salinity-dependent community structure at the phylotype level.

Recovery of OTUs after the application of

different bioinformatics pipelines on HTS data

obtained from an artificial community composed by 22 cyanobacterial strains. Pipelines I – III were carried out using mothur and pipelines IV–V applied UPARSE. OTUs were classified as “Perfect” (identical to a reference sequence), “Good” (≥99% similarity), “Noisy” (≥97.5% to <99% similarity), “Other” (<97.5% similarity), and “Chimeric” (composed of two or more parent reference sequences).


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The role of active site flexible loops in catalysis and of zinc in

conformational stability of Bacillus cereus 569/H/9 β-lactamase Montagner C, Nigen M, Jacquin O, Willet N, Dumoulin M, Karsisiotis AI, Roberts GC, Damblon C, Redfield C, Matagne A. J. Biol. Chem., 31, 16124-16137. doi: 10.1074/jbc.M116.719005, 2016 Metallo-β-lactamases catalyse the hydrolysis of most β-lactam antibiotics and hence represent a major clinical concern. The conformational properties of the BcII β-lactamase have been studied in the presence of chemical denaturants, using a variety of techniques, including enzymatic activity measurement and fluorescence, circular dichroism, and 2D NMR spectroscopies. The data from the various experiments provide evidence that binding of two zinc ions not only increases the conformational stability of the BcII metallo-β-lactamase, but also restores the 3D structural organization that is lost for apoBcII unfolding in the presence denaturant. Moreover, the results highlight the importance of a relatively well-defined conformation for two loops that border the active site in order to maintain enzymatic activity. This study brings new insights into the role of metal cofactors in protein folding as a whole, in the absence of any clinical implications. Moreover, it highlights structural aspects linked to the catalytic activity of the enzyme, which are relevant to inhibitor discovery.

(A) Combined chemical shift differences (CSPs) between 0 and 7.9 M urea, shown as histograms versus the BcII amino acid sequence. The dashed line represents the thresholds (0.0791 ppm) for significant CSPs. With 3 residues (Ile18, Glu37 and Asn118) the signal disappeared completely as urea concentration was increased above 7 M (probably due to exchange broadening); these are indicated with asterisks. Sequence elements corresponding to loops β3-β4 and β11-α4 are indicated; (B) Schematic ribbon representation of the structure where green areas represent those residues undergoing significant CSPs.


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Kinetics of the interaction between BAL29880 and LK157 and the class C

beta-lactamase CHE-1 Fernea A, Galleni M, Frère JM. Antimicrob Agents Chemother, 60, 1747-1750. doi: 10.1128/AAC.02062-15, 2016 The chromosome-encoded class C β-lactamase CHE-1 produced by Enterobacter cloacae exhibits a lower sensitivity to avibactam than the P99 enzyme from which it is derived by a 6-residue deletion in the H-10 helix. In the present study, we investigated the sensitivity of CHE-1 to two other β-lactamase inhibitors: LK-157 (or Lek 157), a tricyclic β-lactam, and BAL29880, a bridged monobactam. With both compounds, the second-order rate constants for inactivation were significantly lower for CHE-1, which can thus be considered an inactivator-resistant mutant of P99. However, the second-order rate constant for the inactivation by BAL29880 probably remains adequate for a rather rapid reaction with CHE-1 in the absence of protection by the substrate.

Variation of ki versus [LK157] for CHE-1.


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Interaction of Avibactam with Class B Metallo-β-Lactamases Abboud MI, Damblon C, Brem J, Smargiasso N, Mercuri P, Gilbert G, Rydzik AM, Claridge TD, Schofield CJ, Frère JM. Antimicrob Agents Chemother. 60(10):5655-62. doi: 10.1128/AAC.00897-16, 2016 β-Lactamases are the most important mechanisms of resistance to the β-lactam antibacterials. There are two mechanistic classes of β-lactamases: the serine β-lactamases (SBLs) and the zinc-dependent metallo-β-lactamases (MBLs). Avibactam, the first clinically useful non-β-lactam β-lactamase inhibitor, is a broad-spectrum SBL inhibitor, which is used in combination with a cephalosporin antibiotic (ceftazidime). There are multiple reports on the interaction of avibactam with SBLs but few such studies with MBLs. We report biochemical and biophysical studies on the binding and reactivity of avibactam with representatives from all 3 MBL subfamilies (B1, B2, and B3). Avibactam has only limited or no activity versus MBL-mediated resistance in pathogens. Avibactam does not inhibit MBLs and binds only weakly to most of the MBLs tested; in some cases, avibactam undergoes slow hydrolysis of one of its urea N-CO bonds followed by loss of CO2, in a process different from that observed with the SBLs studied. The results suggest that while the evolution of MBLs that more efficiently catalyze avibactam hydrolysis should be anticipated, pursuing the development of dual-action SBL and MBL inhibitors based on the diazabicyclooctane core of avibactam may be productive.

Analyses of the hydrolysis reactions of

avibactam with selected MBLs by NMR and Raman spectroscopy. (A) 2D 1H-13C correlation analysis of a mixture of 50% avibactam- and 50% avibactam-hydrolyzed products. Edited HSQC: CH (red), CH2 (pink). HMBC: avibactam pure (green), hydrolysis-avibactam reaction mixture 50:50 (blue). Hydrolysis product signals are in the black boxes in the 2D 1H-13C correlation. The 1D 1H spectrum displayed at the top of the 2D plane corresponds to avibactam (red) and the hydrolysis-avibactam reaction mixture 50/50 (blue). The black labels correspond to the hydrolyzed products. Orange labels correspond to avibactam. (B) Assigned chemical shifts (parts per million) of the products of avibactam VIM-4-mediated hydrolysis are consistent with the products observed with SPM-1 and NDM-1 (2D characterization data not shown). (C) Raman spectroscopic analyses reveal that VIM-4-catalyzed hydrolysis of avibactam proceeds predominantly via simple hydrolysis (and loss of CO2) of the avibactam cyclic urea. Blue trace, VIM-4 and avibactam after 240 min; red trace, same sample spiked with Na2SO4 (the arrow corresponds to Na2SO4).


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Kinetic Studies on CphA Mutants Reveal the Role of the P158-P172 Loop in

Activity versus Carbapenems

Bottoni C, Perilli M, Marcoccia F, Piccirilli A, Pellegrini C, Colapietro M, Sabatini A, Celenza G, Kerff F, Amicosante G, Galleni M and Mercuri PS.

Antimicrob Agents Chemother. 60(5):3123-6, 2016

Site-directed mutagenesis of CphA indicated that prolines in the P158-P172 loop are essential for the stability and the catalytic activity of subclass B2 metallo-β-lactamases against carbapenems. The replacement of single prolines at P158 and P161 led to a strong modification of CphA activities toward carbapenems. A major impact on catalytic efficiencies of the enzyme was observed when the P158A P161A double mutant was generated. The replacement of P161 or P172 yielded an enzyme whose apparent affinity for the second zinc ion increases. This effect was amplified when two or three proline residues were replaced. Therefore, we can conclude that the proline motif plays a structural role in the subclass B2 MBLs. It allows a more rigid and stable structure. It also influences the architecture of the active site and affects the affinity of the second metal binding site.

A. ClustalW alignment of subclass B2 metallo-β-lactamases using Clustal 2.1 multiple-sequence alignment. C. violaceum, Chromobacterium violaceum ATCC 12472; P. ferrooxidans, Pseudogulbenkiania

ferrooxidans; C. piscinae, Chromobacterium piscinae; A. hydrophila CphA, Aeromonas hydrophila CphA; P.

chlororaphis, Pseudomonas chlororaphis; S. Fonticola Sfh-I, Serratia fonticola Sfh-I; Y. mollaretii, Yersinia mollaretii ATCC 43969. B. Comparison of the structures of Sfh-I and CphA. The lateral chains of the amino acids of the P158-P172 loop are shown. C. Influence of the zinc concentrations on the CphA activity. Gray diamond, WT; black square, P158A; plus sign, P161A; gray circle, P172A; black triangle, P158A161A; times sign, P158A161A164A.


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Activity-stability relationships revisited in blue oxidases catalyzing electron

transfer at extreme temperatures.

Roulling F, Godin A, Cipolla A, Collins T, Miyazaki K, Feller G.

Extremophiles 20:621-629. doi: 10.1007/s00792-016-0851-9, 2016

Cuproxidases are a subset of the blue multicopper oxidases that catalyze the oxidation of toxic Cu(I) ions into less harmful Cu(II) in the bacterial periplasm. Cuproxidases from psychrophilic, mesophilic and thermophilic bacteria display the canonical features of temperature adaptation such as increases in structural stability and apparent optimal temperature for activity with environmental temperature as well as increases in the binding affinity for catalytic and substrate copper ions. In contrast, the oxidative activities at 25 °C for both the psychrophilic and thermophilic enzymes are similar, suggesting that the nearly temperature-independent electron transfer rate does not require peculiar adjustments. Furthermore, the structural flexibilities of both the psychrophilic and thermophilic enzymes are also similar, indicating that the firm and precise binding of the four catalytic copper ions is essential for the oxidase function. These results show that the requirements for enzymatic electron transfer, in the absence of the selective pressure of temperature on electron transfer rates, produce a specific adaptive pattern, which is distinct from that observed in enzymes possessing a well-defined active site and relying on conformational changes such as for the induced fit mechanism.

Ribbon diagram of the cuproxidase CueO from E. coli. In magenta, the Met-rich insert binding three Cu(I) ions (orange spheres). According to the proposed mechanism, electrons are transferred from the sCu site (yellow) to the blue T1 copper (blue) and then to the trinuclear center (green) where dioxygen is reduced to water.

Specific activity of cuproxidases. Activity of PhaMOx (circles), CueO (squares) and Tth-MCO (triangles) on 2,6-dimethoxyphenol as a function of Cu(II) concentration at 25 °C.


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Human Chitotriosidase: Catalytic Domain or Carbohydrate Binding

Module, Who's Leading HCHT's Biological Function

Crasson O, Courtade G, Léonard RR, Aachmann FL, Legrand F, Parente R, Baurain D, Galleni M, Sørlie M, Vandevenne M.

Sci Rep. 7(1):2768. doi: 10.1038/s41598-017-02382-z, 2017

Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine units of this biopolymer. HCHT belongs to the Glycoside Hydrolase (GH) superfamily and contains a well-characterized catalytic domain appended to a chitin-binding domain (ChBDCHIT1). Although its precise biological function remains unclear, HCHT has been described to be involved in innate immunity. In this study, the molecular basis for interaction with insoluble chitin as well as with soluble chito-oligosaccharides has been determined. The results suggest a new mechanism as a common binding mode for many Carbohydrate Binding Modules (CBMs). Furthermore, using a phylogenetic approach, we have analysed the modularity of HCHT and investigated the evolutionary paths of its catalytic and chitin binding domains. The phylogenetic analyses indicate that the ChBDCHIT1 domain dictates the biological function of HCHT and not its appended catalytic domain. This observation may also be a general feature of GHs. Altogether, our data have led us to postulate and discuss that HCHT acts as an immune catalyser.

Molecular mechanism of chitin binding and structural features of ChBDCHIT1-49. (A) The diagram shows the chitin binding efficiencies of single mutants generated by directed mutagenesis of predicted binding residues. All the protein mutants (except T452A) displayed reduced binding activities and were classified in three different groups depending on the impact of the mutation: (i) low impact *, (ii) medium impact ** and (iii) high impact ***. (B) X-ray 3D structure of ChBDCHIT1-49 solved by Fadel and coworkers (PDB ID: 5HBF) where the “hevein-fold” motif is shown in surface representation whereas the rest of the structure is represented in cartoon (disulphide bonds are colored in green). Mutated residues were colored in yellow, orange and red depending respectively on the low, medium and high impact of the mutation on the chitin binding function. (C)

90° rotated view of the structure. (D) Detailed view of polar residues (in blue sticks) and Trp465 (in red) in the “hevein-fold” motif of ChBDCHIT1-49 (disulphide bonds in green). (E) Representation of key residues (P451, G453, L454 and V455) involved in the hydrophobic pocket which stabilises Trp465 orientation (disulphide bonds in green). (F) Surface representation of the binding surface of ChBDCHIT1-49 highlighting the key aromatic residue Trp465 and the key polar residues S457, N458, S459, T464 and N458 (blue sticks) directly involved in chitin binding (disulphide bonds in green).


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Crystal structure and biochemical characterization of the transmembrane

PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus

subtilis

Ghachi ME, Howe N, Auger R, Lambion A, Guiseppi A, Delbrassine F, Manat G, Roure S, Peslier S, Sauvage E, Vogeley L, Rengifo-Gonzalez JC, Charlier P, Mengin-Lecreulx D, Foglino M, Touzé T, Caffrey M, Kerff F.

Cell Mol Life Sci. 74(12):2319-2332. doi: 10.1007/s00018-017-2464-6, 2017 Type 2 phosphatidic acid phosphatases (PAP2s) can be either soluble or integral membrane enzymes. In bacteria, integral membrane PAP2s play major roles in the metabolisms of glycerophospholipids, undecaprenyl-phosphate (C55-P) lipid carrier and lipopolysaccharides. By in vivo functional experiments and biochemical characterization we show that the membrane PAP2 coded by the Bacillus subtilis yodM gene is the principal phosphatidylglycerol phosphate (PGP) phosphatase of B. subtilis. We also confirm that this enzyme, renamed bsPgpB, has a weaker activity on C55-PP. Moreover, we solved the crystal structure of bsPgpB at 2.25 Å resolution, with tungstate (a phosphate analog) in the active site. The structure reveals two lipid chains in the active site vicinity, allowing for PGP substrate modeling and molecular dynamic simulation. Site-directed mutagenesis confirmed the residues important for substrate specificity, providing a basis for predicting the lipids preferentially dephosphorylated by membrane PAP2s.

Modeling of bsPgpB complexes and mutation results. (a) Surface electrostatic representation of bsPgpB, with positively and negatively charged regions in blue and red, respectively. The PGP molecule modeled in the bsPgpB active site is shown in yellow and the monoolein molecules present in the bsPgpB structure are shown in black. (b) Cartoon representation of bsPgpB (grey). Residues defining the substrate binding site are displayed as sticks. The PGP and C55-PP molecules modeled in the active site are shown in yellow and green, respectively. Residues modified by site directed mutagenesis in this study are underlined in red. (c) Characterization of bsPgpB mutations in the substrate binding site through phosphatase activity measurements using four different substrates PGP, C55-PP, C15-PP and C5-PP.


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Tracking the Subtle Mutations Driving Host Sensing by the Plant Pathogen

Streptomyces scabies

Jourdan S, Francis IM, Deflandre B, Loria R, Rigali S.

mSphere. 2(2). pii: e00367-16. doi: 10.1128/mSphere.00367-16, 2017

The acquisition of genetic material conferring the arsenal necessary for host virulence is a prerequisite on the path to becoming a plant pathogen. More subtle mutations are also required for the perception of cues signifying the presence of the target host and optimal conditions for colonization. The decision to activate the pathogenic lifestyle is not "taken lightly" and involves efficient systems monitoring environmental conditions. But how can a pathogen trigger the expression of virulence genes in a timely manner if the main signal inducing its pathogenic behavior originates from cellulose, the most abundant polysaccharide on earth? This situation is encountered by Streptomyces scabies, which is responsible for common scab disease on tuber and root crops. We propose here a series of hypotheses of how S. scabies could optimally distinguish whether cello-oligosaccharides originate from decomposing lignocellulose (nutrient sources, saprophyte) or, instead, emanate from living and expanding plant tissue (virulence signals, pathogen) and accordingly adapt its physiological response.

Genetic and physiological

features predicted for the

adaptation of S. scabies to a

pathogenic lifestyle built upon

the perception of cello-oligosaccharides. Factors: 1, disabling of the cellulolytic system; 2, increased affinity of the transporter sugar-binding CebE for cellotriose (root exudates) instead of cellobiose (breakdown of cellulose); 3, fine-tuned control of txtR expression by CebR; 4, posttranscriptional control of txtR by bldA, encoding the leucyl-tRNA for the rare UUA codon. nt, nucleotides.


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Cyanobacterial Contribution to Travertine Deposition in the Hoyoux River

System, Belgium

Kleinteich J, Golubic S, Pessi IS, Velázquez D, Storme JY, Darchambeau F, Borges AV, Compère P, Radtke G, Lee SJ, Javaux EJ, Wilmotte A.

Microb Ecol. 74(1):33-53. doi: 10.1007/s00248-017-0937-7, 2017

Travertine deposition is a landscape-forming process, usually building a series of calcareous barriers differentiating the river flow into a series of cascades and ponds. The process of carbonate precipitation is a complex relationship between biogenic and abiotic causative agents, involving adapted microbial assemblages but also requiring high levels of carbonate saturation, spontaneous degassing of carbon dioxide and slightly alkaline pH. We have analysed calcareous crusts and water chemistry from four sampling sites along the Hoyoux River and its Triffoy tributary (Belgium) in winter, spring, summer and autumn 2014. Different surface textures of travertine deposits correlated with particular microenvironments and were influenced by the local water flow. In all microenvironments, we have identified the cyanobacterium Phormidium incrustatum (Nägeli) Gomont as the organism primarily responsible for carbonate precipitation and travertine fabric by combining morphological analysis with molecular sequencing (16S rRNA gene and ITS, the Internal Transcribed Spacer fragments), targeting both field populations and cultures to exclude opportunistic microorganisms responding favourably to culture conditions. Several closely related cyanobacterial strains were cultured; however, only one proved identical with the sequences obtained from the field population by direct PCR. This strain was the dominant primary producer in the calcareous deposits under study and in similar streams in Europe. The dominance of one organism that had a demonstrated association with carbonate precipitation presented a valuable opportunity to study its function in construction, preservation and fossilisation potential of ambient temperature travertine deposits. These relationships were examined using scanning electron microscopy and Raman microspectroscopy.

1. Travertine barriers. 2. Direct Scanning Electron Microscope picture of the opening of calcareous tubule with the exiting cyanobacterial trichome. 3. Cyanobacterial Phormidium strains detected in the Hoyoux travertine


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Interplay between Penicillin-binding proteins and SEDS proteins promotes

bacterial cell wall synthesis

Leclercq S, Derouaux A, Olatunji S, Fraipont C, Egan AJ, Vollmer W, Breukink E, Terrak M

Sci Rep. 7:43306. doi: 10.1038/srep43306, 2017 Bacteria utilize specialized multi-protein machineries to synthesize the essential peptidoglycan (PG) cell wall during growth and division. The divisome controls septal PG synthesis and separation of daughter cells. In E. coli, the lipid II transporter candidate FtsW is thought to work in concert with the PG synthases penicillin-binding proteins PBP3 and PBP1b. Yet, the exact molecular mechanisms of their function in complexes are largely unknown. We show that FtsW interacts with PBP1b and lipid II and that PBP1b, FtsW and PBP3 co-purify suggesting that they form a trimeric complex. We also show that the large loop between transmembrane helices 7 and 8 of FtsW is important for the interaction with PBP3. Moreover, we found that FtsW, but not the other flippase candidate MurJ, impairs lipid II polymerization and peptide cross-linking activities of PBP1b, and that PBP3 relieves these inhibitory effects. All together the results suggest that FtsW interacts with lipid II preventing its polymerization by PBP1b unless PBP3 is also present, indicating that PBP3 facilitates lipid II release and/or its transfer to PBP1b after transport across the cytoplasmic membrane. This tight regulatory mechanism is consistent with the cell's need to ensure appropriate use of the limited pool of lipid II.

Left panel. Schematic representation of the septal peptidoglycan synthesis core of the divisome. The proteins studied in this paper are shown in color the others are in grey. TP, transpeptidase domain; GT, glycosyltransferase domain; L and B stand for FtsL and FtsB respectively; n-PBD, non-penicillin binding domain. Right Panel. Effect of FtsW, PBP3 and the FtsW-PBP3 complex on the polymerization of lipid II

by PBP1b as revealed by the continuous florescence assay. The fluorescence of dansyl-lipid II decreases over time upon polymerization by PBP1b. A. inhibition of lipid II polymerization by FtsW from E. coli, S. enterica and K. pneumoniae. B. in contrast to FtsW (5µM), the polymerase activity of PBP1b is not inhibited by the FtsW-PBP3 complex (5µM) and slightly decreases in the presence of PBP3 (5µM). C. PBP1b activation by LpoB (200 nM) does not suppress the inhibitory effect of FtsW (5µM). D. in contrast to FtsW, MurJ (0.5-5µM) has no effect on the polymerase activity of PBP1b.


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Assessment of the Potential Role of Streptomyces in Cave Moonmilk

Formation

Maciejewska M, Adam D, Naômé A, Martinet L, Tenconi E, Całusińska M, Delfosse P, Hanikenne M, Baurain D, Compère P, Carnol M, Barton HA, Rigali S.

Front Microbiol. 8:1181. doi: 10.3389/fmicb.2017.01181, 2017

Moonmilk is a karstic speleothem mainly composed of fine calcium carbonate crystals (CaCO3) with different textures ranging from pasty to hard, in which the contribution of biotic rock-building processes is presumed to involve indigenous microorganisms. The real microbial input in the genesis of moonmilk is difficult to assess leading to controversial hypotheses explaining the origins and the mechanisms (biotic vs. abiotic) involved. In this work, we undertook a comprehensive approach in order to assess the potential role of filamentous bacteria, particularly a collection of moonmilk-originating Streptomyces, in the genesis of this speleothem. Scanning electron microscopy (SEM) confirmed that indigenous filamentous bacteria could indeed participate in moonmilk development by serving as nucleation sites for CaCO3 deposition. The metabolic activities involved in CaCO3 transformation were furthermore assessed in vitro among the collection of moonmilk Streptomyces, which revealed that peptides/amino acids ammonification, and to a lesser extend ureolysis, could be privileged metabolic pathways participating in carbonate precipitation by increasing the pH of the bacterial environment. Additionally, in silico search for the genes involved in biomineralization processes including ureolysis, dissimilatory nitrate reduction to ammonia, active calcium ion transport, and reversible hydration of CO2 allowed to identify genetic predispositions for carbonate precipitation in Streptomyces. Finally, their biomineralization abilities were confirmed by environmental SEM, which allowed to visualize the formation of abundant mineral deposits under laboratory conditions. Overall, our study provides novel evidences that filamentous Actinobacteria could be key protagonists in the genesis of moonmilk through a wide spectrum of biomineralization processes.

Heterotrophic pathways associated with carbonatogenesis presumed to occur in Streptomyces species.


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The proteolytic system of pineapple stems revisited: purification and

characterization of multiple catalytically active forms

Matagne A, Bolle L, El Mahyaoui R, Baeyens-Volant D, Azarkan M.

Phytochemistry, 138, 29-51, 2017

Crude pineapple proteases extract (aka stem bromelain; EC 3.4.22.4) is an important proteolytic mixture that contains enzymes belonging to the cysteine proteases of the papain family. Numerous studies have been reported aiming at the fractionation and characterization of the many molecular species present in the extract, but more efforts are still required to obtain sufficient quantities of the various purified protease forms for detailed physicochemical, enzymatic and structural characterization. In this work, we describe an efficient strategy towards the purification of at least eight enzymatic forms. Thus, following rapid fractionation on a SP-Sepharose FF column, two sub-populations with proteolytic activity were obtained: the unbound (termed acidic) and bound (termed basic) bromelain fractions. Following reversible modification with mPEG, both fractions were further separated on Q-Sepharose FF and SP-Sepharose FF, respectively. This procedure yielded highly purified molecular species, all titrating ca. 1 mol of thiol group per mole of enzyme, with distinct biochemical properties. N-terminal sequencing allowed identifying at least eight forms with proteolytic activity. The basic fraction contained previously identified species, i.e. basic bromelain forms 1 and 2, ananain forms 1 and 2, and comosain. Furthermore, a new proteolytic species, showing similarities with basic bomelain forms 1 and 2, was discovered and termed bromelain form 3. The two remaining species were found in the acidic bromelain fraction and were arbitrarily named acidic bromelain forms 1 and 2. Both, acidic bromelain forms 1, 2 and basic bromelain forms 1, 2 and 3 are glycosylated, while ananain forms 1 and 2, and comosain are not. The eight protease forms display different amidase activities against the various substrates tested, namely small synthetic chromogenic compounds, fluorogenic compounds, and proteins, suggesting a specific organization of their catalytic residues. All forms are completely inhibited by specific cysteine and cysteine/serine protease inhibitors, but not by specific serine and aspartic protease inhibitors, with the sole exception of pepstatin A that significantly affects acidic bromelain forms 1 and 2. For all eight protease forms, inhibition is also observed with 1,10-phenanthrolin, a metalloprotease inhibitor. Metal ions (i.e. Mn2+, Mg2+ and Ca2+) showed various effects depending on the protease under consideration, but all of them are totally inhibited in the presence of Zn2+. Mass spectrometry analyses revealed that all forms have a molecular mass of ca. 24 kDa, which is characteristic of enzymes belonging to the papain-like proteases family. Far-UV CD spectra analysis further supported this analysis. Interestingly, secondary structure calculation proves to be highly reproducible for all cysteine proteases of the papain family tested so far (see Table below) and thus can be used as a test for rapid identification of the classical papain fold. Table. Calculated secondary structure derived from far-UV CD data

Helices Strands Turns Unordered Papain(1) 20 ± 3 25 ± 5 18 ± 1 38 ± 4 Caricain(1) 19 ± 2 22 ± 3 15 ± 5 42 ± 6 Ficin A(1) 19 ± 1.5 26 ± 3 19 ± 1.5 35 ± 4 Ficin B(1) 19 ± 2 24 ± 5 18 ± 1.5 40 ± 6 Ficin C(1) 24 ± 4 22 ± 2 18 ± 2 36 ± 3 Ficin D1(1) 23 ± 3 23 ± 5 18 ± 2 37 ± 7 Ficin D2(1) 23 ± 3 22 ± 3 18 ± 2 37 ± 3 Ficin E(2) 22 ± 2 26 ± 4 18 ± 2 35 ± 4 Basic Bromelain 1(3) 18 ± 2 28 ± 6 21 ± 1 33 ± 5 Basic Bromelain 2(3) 22 ± 1 24 ± 2 21 ± 1 33 ± 3 Basic Bromelain 3(3) 21 ± 2 24 ± 4 20 ± 3 35 ± 6 Average 21 ± 2 24 ± 2 18.5 ± 2.0 36 ± 3

(1) Azarkan et alI (2011); (2) Baeyens-Volant et al. (2015); (3) This work


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Cryosphere and Psychrophiles: Insights into a Cold Origin of Life?

Feller G. Life 7:25. DOI: 10.3390/life7020025 Psychrophiles thrive permanently in the various cold environments on Earth. Their unsuspected ability to remain metabolically active in the most extreme low temperature conditions provides insights into a possible cold step in the origin of life. More specifically, metabolically active psychrophilic bacteria have been observed at −20 °C in the ice eutectic phase (i.e., the liquid veins between sea ice crystals). In the context of the RNA world hypothesis, this ice eutectic phase would have provided stability to the RNA molecules and confinement of the molecules in order to react and replicate. This aspect has been convincingly tested by laboratory experiments.

Bacteria visualized microscopically directly within a brine pocket of Arctic winter sea ice at −15 °C. (a) The transmitted light image shows ice crystals and the brine-filled veins between them; (b) Enlarged image of a brine pocket in (a) shows the microscale habitat; (c) Its bacterial inhabitants are revealed

by epifluorescence microscopy (Deming, 2002), reprinted by permission from Elsevier.

SCIENTIFIC SERVICES

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CONTACTS BCCM/ULC: Culture collection for cyanobacteria : http://bccm.belspo.be/about-us/bccm-ulc Manager: Dr Annick Wilmotte: [email protected] Tel: + 32 (0) 4 366 33 87 / 38 56 Technical assistance: Kim Beets: [email protected] Tel: + 32 (0) 4 366 33 87 Protein Factory : http://www.proteinfactory.ulg.ac.be/ Manager: Dr Alain Brans: [email protected] Tel: + 32 (0) 4 366 34 50 Collaborators: Fabrice Bouillenne, Anne-Marie Matton and Iris Thamm

Robotein®

Dr André Matagne : [email protected]

Tel : + 32 (0) 4 366 34 19

Dr Alain Brans : [email protected] Tel: + 32 (0) 4 366 34 50

Dr Julie Vandenameele: [email protected] Tel: + 32 (0) 4 366 35 04 Training: “Techniques for protein production and purification” Biotechnology Training Centre: Laurent Corbesier: [email protected] www.formation-biotechnologie.be Tel : + 32 (0) 4 366 39 00 Dr Alain Brans : [email protected] Tel: + 32 (0) 4 366 34 50 Fabrice Bouillenne : [email protected]

Tel: + 32 (0) 4 366 33 15

SCIENTIFIC SERVICES

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BCCM/ULC

A CULTURE COLLECTION OF CYANOBACTERIA Since 2005, the BCCM (Belgian Co-ordinated Collections of Microorganisms) has supported the

elaboration of a collection of cyanobacteria. The integration towards an official public collection,

called BCCM/ULC, was completed in 2011. The BCCM/ULC public collection of cyanobacteria focusses on the “ex situ” conservation of a representative portion of the polar cyanobacterial diversity with different origins, isolated from terrestrial (e.g. soil crusts, cryoconites, endoliths) and aquatic ecosystems (e.g. limnetic microbial mats, freshwater lakes and marine environments). BCCM ULC currently holds 175 cyanobacterial strains, including over 100 of polar origin (catalogue: http://bccm.belspo/catalogues/ulc-catalogue-search). The strains are available for researchers who study taxonomy, evolution, biogeography, adaptation to harsh environmental conditions, production of bioactive compounds, etc. Morphological and molecular identifications (based on SSU rRNA sequences) indicate that the strains belong to the orders Synechococcales, Oscillatoriales, Pleurocapsales, Chroococcidiopsidales and Nostocales. This large taxonomic distribution makes the collection interesting for phylogenomic and genomic make-up studies, hence the genome sequencing of several strains is ongoing. Continuous maintenance of living cultures ensures the preservation of strains, of which the majority are cryopreserved (as back-up at -70°C) in order to limit the genetic drift. BCCM/ULC obtained an ISO 9001:2015 certification for public and safe deposits, and distributions of strains, as part of the multi-site certification for the Belgian Coordinated Collections of Microorganisms (BCCM) consortium. Other services are available, like the delivery of genomic DNA and culture media. On the basis of our taxonomic expertise, a new service of molecular identification is also proposed. Trainings in preservation, cultivation and characterization are organized each year. The policies of acquisition and distribution of the collection are translated respectively into contracts called Material Accession Agreements (MAA) and Material Transfer Agreements (MTA). This guarantees safe “fit-for-use” microbiological material and data compliant with the rules on access and utilization of the Nagoya Protocol under the Convention on Biological Diversity (12 October2014). The molecular characterization of the strains is underway, on the basis of 16S rRNA and ITS sequences. The genome of the first axenic Antarctic cyanobacterial strain, ULC007, was determined (Lara et al. 2017) and other genome sequencings are underway. BCCM/ULC progressively incorporates the most interesting strains from the research collection of the host laboratory into the public collection. In addition, it is also enriched by public deposits from other geographical areas.

SCIENTIFIC SERVICES

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PROTEIN FACTORY FOR PROTEIN PRODUCTION AND PURIFICATION

An effective research requires access to a broad range of technologies, some of which require

expertise and specific equipments. Protein Factory is a protein production platform for

academic laboratories and private companies. One of the objectives of the platform is to provide

laboratory and pilot-scaled equipment for on- and off-campus users. Services include protein

production in bacterial, yeast and filamentous fungal strains, followed by their purification. The platform can provide many services including: The genetic engineering and cloning in bacterial strains such as E. coli, Bacillus subtilis,

Streptomyces lividans or in yeast such as Pichia pastoris The analytical scale or pilot scale recombinant protein production from these organisms Colony picking High throughput culture condition screening High cell density fermentation Cell harvesting or supernatant cleaning using bucket or continuous centrifugation or hollow fiber

filtration Cell disintegration to recover proteins produced in the intracellular compartment Protein purification at the analytical and pilot scales.

For these purposes the platform is equipped with: Several shaking incubators for microtitre plates to 2 L flasks Wide range of computer controlled fermentors with working volumes from 5 to 80 L for batch and

fed-batch cultures. Dissolved oxygen, pH, temperature, agitation and turbidity are controlled in all fermentors

1 bucket and 1 continuous centrifuges 2 crossflow filtration unit Several systems for semi- or totally automated purification of proteins including: ÅKTA prime,

ÅKTA explorer, ÅKTA explorer (2D system), ÅKTA purifier, Biopilot, Profinia Protein Purification System, NGC systems.

Protein Factory has provided proteins for: kinetic studies, protein structure determination by NMR or crystallography, protein-protein or protein-ligand interaction studies, secondary metabolite productions, enzyme-inhibitor studies, amyloid fibril formation and protein folding studies, immunoassay developments, vaccination studies and immuno test kit manufacturing.

SCIENTIFIC SERVICES

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HIGH-THROUGHPUT PROTEIN PRODUCTION AND ANALYSIS

Robotein is a versatile technological platform for high-throughput (HT) protein production and analysis. It is built on the competences and infrastructures available in the academic setting of two labs that offer a complete structural biology portfolio: the Centre for Protein Engineering at the University of Liège and the Structural Biology and Bioinformatics Centre at the Université Libre de Bruxelles. We develop protocols for (HT) cloning, mutagenesis and colony picking (E. coli and Pichia cells), screening for production of recombinant proteins (selection of the best producers, screening for optimal culture medium, enhanced reproducibility and yield at each purification step), biophysical characterization (e.g. automated screening of refolding conditions and conformational stability measurements, quantitative analysis of hundreds of proteins using infrared spectroscopy), label-free interaction analysis, and enzymatic assays. We offer automated screening for cloning, gene expression, purification and biophysical analysis on either a collaborative or service basis. European scientists can get access to Robotein through the European Commission funded Instruct Internship programme. The HT screening approach serves to optimize the labour intensive downstream steps, i.e. large-scale production and detailed biochemical and biophysical studies. Robotein is equipped with two robotic workstations of the Microlab STAR line by Hamilton, two microplate readers (Infinite M200 PRO by Tecan) allowing UV/Vis absorbance and fluorescence measurements, together with chemiluminescence detection, a system (LabChip GXII, by Perkin Elmer) for automated electrophoretic separation of nucleic acids and proteins, an Octet HTX platform (fortéBio – Pall Life Sciences) allowing HT analysis of biomolecular interactions and quantitation of biomolecules even in crude extracts, in 96- and 384-well microplates. Furthermore, the combination of a protein spotter (Arrayjet Marathon Classic microarrayer) with an infrared imager (128x128 focal plane array detector Agilent FTIR imaging microscope) allows fast and reliable quantification of many protein samples, together with determination of protein secondary structure content and measurement of phosphorylations and glycosylations.

SCIENTIFIC SERVICES

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Techniques for protein production and purification

Since 2006, the CIP works in close collaboration with the Biotechnology Training Centre Forem-GIGA to develop and organize biotechnology training for jobseekers in the field of protein production and purification. At the CIP, the training includes the following technological modules: Bacterial transformation (Escherichia coli and Bacillus subtilis)

Protein production in flasks and in 20 L fermentors (batch and fed-batch cultures) with E. coli, B.

subtilis and P. pastoris

Cell harvesting and cell disruption

Protein purification by different chromatography technologies including: ion exchange, molecular sieve, hydrophobic and affinity chromatographies

Protein identification by SDS-PAGE, enzymatic testing and Western blotting.

SCIENTIFIC PRODUCTION

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AWARDS A. Wilmotte, Nomination as Belgian Woman Scientist to participate to the Wikibomb organised by the Scientific Committee on Antarctic Research (SCAR). Wikipedia profile written and published: https://en.wikipedia.org/wiki/Annick_Wilmotte, 2016

L. Martinet, BSMS 2017 Poster Award, "Streptomyces from Moonmilk, an untapped source of new bioactive compounds" XXth annual meeting, Leuven, Belgium, February 08, 2017 L. Martinet, Best Poster Award, "Screening of bioactive compounds produced by karstic streptomices", PhD student Day, Liège, Belgium, May 11, 2017 L. Martinet, Diplôme du meilleur oral junior, Colloque Actino 2017, Journées des actinobactéries, Lyon, France, October 20, 2017


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INVITED SPEAKERS – 2016 Dr Elisa Beneventi, University of Padova, Italy,"Production and structural characterization of a new dual cofactor-specific formate dehydrogenase from Granulicella mallensis MP5ACTX8", January 26 Dr Xavier de Bolle, University of Namur, Belgium, "Survival, growth and replication of the intracellular pathogen Brucella abortus", March 11 Dr Han Remaut, University of Brussels, Belgium, "Amyloid secretion and assembly: the bacterial way", June 3 Dr Alessandra Corazza, University of Udine, Italy, “Interactions in amyloidogenic proteins: a possible role in fibril formation”, June 16 Dr Yves Engelborghs, University of Leuven, Belgium, "A physical meaning of the Lineweaver-Burk equation ", October 7 Dr Pierrette Melin, CHU of Liège, Belgium, “Multi-résistance aux antibiotiques chez les Bacilles Gram négatif en 2016 - Ampleur du problème, impact clinique et moyens de diagnostic”, October 28 Dr Rita Vanbeverre, University of Louvain, Belgium, "Protein PEGylation for the sustained residence time of proteins in the lungs", November 25 Dr Alexander Tischer, Mayo Clinic, Rochester, USA, "Von Willebrand disease - What protein folding can teach us to understand a common bleeding disorder", December 6 Dr Denis Baurain, University of Liège, Belgium, "Probing publicly available cyanobacterial genomes for contaminating sequences", December 16

INVITED SPEAKERS – 2017 Prof. Yves Briers, Faculty of Bioscience Engineering, University of Ghent, Belgium, “Artilysins and L-forms: a story about cell walls, January 26 Dr Patrick England, Institut Pasteur, Paris, France, “Quantitative molecular-scale biophysics in the Institut Pasteur: the role of the molecular biophysics facility”, March 9 Dr Vincent Forge, Biosciences and Biotechnology Institute of Grenoble, LCBM, CEA Grenoble, France, “Self-assembling proteins for bio-inspired nano-electronics”, June 2 Dr Kaori Okhi, Dpt of Marine Bioscience, Fukui Prefectural University, Obama, Fukui, Japan, “Exopolysaccharide production by the fresh-water cyanobacterium Aphanothece

sacrum (Suizenji Nori) that has been cultured as a food source in Japan”, June 12


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Prof. Arnout Voet, KUL, Leuven, Belgium, “A RE3volutionary design of symmetric protein building blocks”, September 22 Dr Marie A.M. Renault, University of Utrecht, The Netherlands, “Structural basis of O-mycoloylated protein targeting the mycomembrane”, October 27 Prof. J. Elster, Centre for Polar Ecology, Faculty of Science, University of South Bohemia and Centre for Algology, Institute of Botany, CAS, Trebon, Czech Republic, “Development of low temperature algal biotechnology”, November 30

Dr Mathieu Surin, University of Mons, Belgium, “Supramolecular DNA assemblies: from structure to the chiroptical readout of the enzymatic activity”, December 8


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ORAL PRESENTATIONS – 2016

A. Matagne, Flash presentation entitled “Robotein®, a robotic platform for high throughput protein production and analysis”, The Astbury Conversation, Understanding the secret life of molecules, University of Leeds, UK, April 11-12 S. Rigali, “One click… and an herbicide onto the market! Greenwin: white biotechnology: from research to industrial applications”, ULg, Gembloux, Belgium, May 13 A. Matagne, “Zinc as a key player in metallo-β-lactamase activity and stability”, Laboratoire de Signalisation et Récepteurs Matriciels (SiRMa), Université de Reims Champagne-Ardenne, France, June 7

A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase”, The Fourth Edition of International Conference on Analytical and Nanoanalytical Methods for Biomedical and Environmental Sciences IC-ANMBES 2016, Brasov, Romania, June 29 – July 1 A. Wilmotte, “Inviolate areas to protect reference sites for future microbiology research in Antarctica”, 34th Scientific Committee on Antarctic Research (SCAR), Biennal Meetings, Kuala Lumpur, Malaysia, August 20-27 A. Wilmotte, “Diversity and distribution of microorganisms in microbial mats of Antarctic lakes”, 34th Scientific Committee on Antarctic Research (SCAR), Biennal Meetings, Kuala Lumpur, Malaysia, August 20-27 I. S. Pessi, “Successional trajectories of cyanobacterial communities following glacier retreat in Svalbard (High Arctic) ”, 20th Cyanophyte/Cyanobacteria Research Symposium, University of Innsbruck, Innsbruck, Austria, August 28 – September 02 F. Kerff, “Structure of the class D beta-lactamase OXA-29, an original dimer”, 23th Congresso Latinoamericano de Microbiologia, Rosario, Argentina, September 29 JM Frère, “Penicillin Binding Proteins”, Advanced Course on Antibiotics, Fondation Mérieux, Nancy, France, October 11 G. Feller, “DSC of Extremophilic Proteins, a Case Study”, Liège, Belgium, November 22 M. Dumoulin, “Mechanism of aggregation of polyglutamine (polyQ) proteins which are associated with neurodegenerative amyloidosis. Creation and characterization of polyQ hybrid proteins made from the beta-lactamase BlaP”, Louvain Drug Research Institute, UCL, Belgium, December 5


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ORAL PRESENTATIONS – 2017 A. Matagne, “Joint initiative on the quality of recombinant proteins – Improving the time-efficiency and quality of your results - Implementation of a standardized sample quality control workflow, Eurogentec, Liège, Belgium, February 15 A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase” ARBRE-MOBIEU plenary meeting – Building Bridges in Biophysics Instituto de Investigação em Saúde, Porto, Portugal, March 22-24

I.S. Pessi, “Successional Dynamics of Cyanobacterial Communities Following the Retreat of

Two Glaciers in Petunia Bay (Svalbard)”, The Arctic Science Summit Week, Prague, Czech

Republic, April 1-7

F. Kerff, "Bacterial phosphatases of the PAP2 family active on membrane lipids, structures

and specificity", Mini-symposium « The cell envelope of Gram-negative bacteria », Brussels,

Belgium, April 21

M. Dumoulin, “Switching to the dark side : repositioning of polyglutamine repeat promotes

amyloid fibril formation by the model protein, β-Lactamase BlaP”, Biophysical Seminars,

Department of Chemistry, University of Cambridge, Cambridge, UK, May 3

A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase”, Laboratory of Biochemistry, University of Wageningen, The Netherlands, May 12 A. Matagne, “30 year at the University. What about collaboration?” Workshop on “Getting the most out of your collaborations” organized by the VIB Postdoc community KUL, Leuven, Belgium, June 6 A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase” 13th β-lactamase meeting, Santo Stefano di Sessanio (L’Aquila), Italy, June 16-19

JM Frère, “Avibactam and class B enzymes”, 13th -lactamase meeting, L’Aquila, Italy, June 17 A. Wilmotte, “Antarctic cyanobacteria: from diversity to genomics”, Marine Microorganisms and their Contribution to Global Biogeochemical Cycles, Symposium in honour of Professor Lucas Stal, Amsterdam, The Netherlands, June 30

A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase”, Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris Sud, Orsay, France, July 6


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B. Durieu, “Biogeographic patterns and genomic adaptation of benthic cyanobacteria in

Antarctic lakes”, XIIth SCAR Biology Symposium, Leuveun, Belgium, July 10-14

I.S. Pessi, “Succession of microbial photoautotrophs along a soil chronosequence in maritime Antarctica”, XIIth SCAR Biology Symposium, Leuveun, Belgium, July 10-14

A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase” 11th International Conference “Processes in Isotopes and Molecules”, INCDTIM Cluj-Napoca, Romania, September 27-29 A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase”, Institut de Biologie et Médcine Moléculaire, Département de Biologie Moléculaire, Université Libre de Bruxelles, Gosselies, Belgium, October 13 S. Rigali, “Tracking the Subtle Mutations Thriving Host Sensing by the Plant Pathogen Streptomyces scabies”, Actino2017, Lyon, France, October 18 A. Matagne, “The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-lactamase”, Chemistry Institute, Ljubljana, Slovenia, November 17


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PHD THESES 13/01/2016 Clémentine Laurent (Sciences) Caractérisation des motifs structuraux modulant l’affinité du transporteur

HMA4 d’Arabidopsis halleri pour les métaux 22/06/2016 Adriana Herteg-Fernea (Chimie) Caractérisation du spectre d’action de la bêta-lactamase de classe C, CHE-1 09/09/2016 Régine Freichels (Sciences) Caractérisation biochimique et structurale des tagatose-1,6-bisphosphate

aldolases de classe I d’origine procaryotique 26/09/2016 Samuel Jourdan (Sciences) Mécanismes moléculaires associés à l’induction de la pathogénicité chez

Streptomyces scabies 28/11/2016 Maxime Maréchal (Sciences) Etude de la régulation de l’expression de l’opéron ftsW-psr-pbp5 chez

Enterococcus hirae

14/12/2016 Ismahene Dahmane (Sciences) Etude des glycosyltransférases (GTs) responsables de la polymérisation du

peptidoglycane et inhibition de leur activité 30/03/2017 Sarah Lebrun (Sciences) Génération d’une librairie de mutants de Bacillus licheniformis 749/I par

l’insertion aléatoire d’un transposon pour identifier les gènes impliqués dans l’induction de la bêta-lactamase BlaP

31/03/2017 Marta Maciejewska (Sciences) Diversity, ecology and antimicrobial properties of moonmilk indigenous

actinobacteria 26/04/2017 Edwige Van der Heiden (Sciences) Utilisation du D-galactose et du D-tagatose chez Bacillus sp. – Etude des

protéines GalM et PBP4 de B. Subtilis et de B. amyloliquefaciens et étude de la voie catabolique PTS-dépendante du D-tagatose chez B. licheniformis

05/09/2017 Igor Stelmach Pessi (Sciences) The cyanobacterial biota of Polar regions: a molecular approach 08/12/2017 Bathabile Ramalapa (Sciences) Design of new delivery systems for therapeutic proteins based on calcium

carbonate microspheres


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PUBLICATIONS 2016 MI Abboud, C. Damblon, J. Brem, N. Smargiasso, P. Mercuri, B. Gilbert, AM Rydzik, TD Claridge, CJ Schofield and JM Frère Interaction of avibactam with class B metallo-beta-lactamases Antimicrob Agents Chemother, 60, 5655-5562 R. Abrashev, G. Feller, N. Kostadinova, E. Krumova, Z. Alexieva, M. Gerginova, B. Spasova, J. Miteva-Staleva, S. Vassilev and M. Angelova Production, purification, and characterization of a novel cold-active superoxide dismutase from the Antarctic strain Aspergillus glaucus 363 Fungal Biology, 120, 679-689

M. Ahn, C. L. Hagan, A. Bernardo-Gancedo, E. De Genst, F. N. Newby, J. Christodoulou, A. Dhulesia, M. Dumoulin, C. V. Robinson, C. M. Dobson and J. R. Kumita The significance of the location of mutations for the native-state dynamics of human lysozyme Biophys. J., 111, 2358-2367 D. Baurain, A. Wilmotte and JM Frère Gram-negative bacteria: “inner” vs “cytoplasmic” or “plasma membrane”: a question of clarity rather than vocabulary J. Microb. Biochem. Technol., 8, 325-326

C. Bottoni, M. Perilli, F. Marcoccia, A. Piccirilli, C. Pellegrini, M. Colapietro, A. Sabatini, G. Celenza, F. Kerff, G. Amicosante, M. Galleni and PS Mercuri Kinetic studies on CphA mutants reveal the role of the P158-P172 loop in activity versus carbapenems Antimicrob Agents Chemother, 60, 3123-3126 G. Claisse, G. Feller, M. Bonneau and JL Da Lage A single amino-acid substitution toggles chloride dependence of the alpha-amylase paralog amyrel in Drosophilia melanogaster and Drosophilia virilis species Insect Biochem. Mol. Biol., 75, 70-77

JP Descy, F. Leprieur, S. Pirlot, B. Leporcq, J. Van Wichelen, A. Peretyatko, S. Teissier, GA Codd, L. Triest, W. Vyverman and A. Wilmotte Identifying the factors determining blooms of cyanobacteria in a set of shallow lakes Ecol. Inform., 34, 129-138

A. Fernea, M. Galleni and JM Frère Kinetics of the interaction between BAL29880 and LK157 and the class C beta-lactamase CHE-1 Antimicrob Agents Chemother, 60, 1747-1750

M. Figueroa, M. Sleutel, M. Vandevenne, G. Parvizi, S. Attout, O. Jacquin, J. Vandenameele, A.W. Fischer, C. Damblon, E. Goormaghtigh, M. Valerio-Lepiniec, A. Urvoas, D. Durand, E. Pardon, J. Steyaert, P. Minard, D. Maes, J. Meiler, A. Matagne, J. A. Martial and C. Van de Weerdt


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The unexpected structure of the designed protein Octarellin V.1 forms a challenge for protein structure prediction tools J. Struct. Biol., 195, 19-30

M. Figueroa, J. Vandenameele, E. Goormaghtigh, M. Valerio-Lepiniec, P. Minard, A. Matagne and C. Van de Weerdt Biophysical characterization data of the artificial protein Octarellin V.1 and binding test with its X-ray helpers Data in Brief, 8, 1221-1226

JM Frère, E. Sauvage and F. Kerff From “An enzyme able to destroy penicillin” to carbapenemases: 70 years of beta-lactamase misbehavior Curr. Drug Targets, 17, 974-982

S. Jourdan, IM Francis, MJ Kim, JJC Salazar, S. Planckaert, JM Frère, A. Matagne, F. Kerff, B. Devreese, R. Loria and S. Rigali The CebE/MsiK transporter is a doorway to the cello-oligosaccharide-mediated induction of Streptomyces scabies pathogenicity Sci. Rep., doi: 10.1038/srep27144

C. Laurent, G. Lekeux, A.A. Ukuwela, Z. Xiao, JB Charlier, B. Bosman, M. Carnol, P. Motte, C. Damblon, M. Galleni and M. Hanikenne Metal binding to the N-terminal cytoplasmic domain of the PIB ATPase HMA4 is required for metal transport in Arabidopsis Plant Mol Biol, 90, 453-466

S.T. Lefurgy, V.N. Malashkevich, J.T. Aguillan, E. Nieves, E.C. Mundorff, B. Biju, M.A. Noel, R. Toro, D. Baiwir, K.M. Papp-Wallace, S.C. Almo, J-M Frère, G. Bou and R.A. Bonomo Analys of the structure and function of FOX-4 cephamycinase Antimicrob Agents Chemother, 60, 717-728

M. Maciejewska, D. Adam, L. Martinet, A. Naômé, M. Calusinska, P. Delfosse, M. Carnol, HA Barton, MP Hayette, N. Smargiasso, E. De Pauw, M. Hanikenne, D. Baurain and S. Rigali A phenotypic and genotypic analysis of the antimicrobial potential of cultivable Streptomyces isolated from cave moonmilk deposits Front. Microbiol, 7, doi:10.3389/fmcb.2016.01455

F. Marcoccia, C. Bottoni, A. Sabatini, M. Colapietro, P.S. Mercuri, M. Galleni, F. Kerff, A. Matagne, G. Celenza, G. Amicosante and M. Perilli Kinetic study of laboratory mutants of NDM-1 metallo-beta-lactamase and the importance of an isoleucine at position 35 Antimicrob Agents Chemother, 60, 2366-2372 M. Maréchal, A. Amoroso, C. Morlot, T. Vernet, J. Coyette and B. Joris Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site BMC Microbiology, 16:39 DOI10.1186/s12866-016-0844-y


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C. Michaux, G. Roussel, M. Lopes-Rodrigues, A. Matagne and E.A. Perpète Unravelling the mechanisms of a protein refolding process based on the association of detergents and co-solvents J. Pept. Sci., DOI 10.1002/psc.2893 C. Montagner, M. Nigen, O. Jacquin, N. Willet, M. Dumoulin, AI Karsisiotis, GCK Roberts, C. Damblon, C. Redfield and A. Matagne The role of active site flexible loops in catalysis and of zinc in conformational stability of Bacillus cereus 569/H/9 beta-lactamase J. Biol. Chem., 31, 16124-16137 D.A. Pearce, I.A. Alekhina, A. Terauds, A. Wilmotte, A. Quesada, A. Edwards, A. Dommergue, B. Sattler, B.J. Adams, C. Magalhães, W-L Chu, M.C.Y. Lau,C. Cary, D.J. Smith, D.H. Wall, G. Eguren, G. Matcher, J.A. Bradley, J-P de Vera, J. Elster, K.A. Hughes,L. Cuthbertson, L.G. Benning, N. Gunde-Cimerman, P. Convey, S.G. Hong, S.B. Pointing, V.H. Pellizari and W.F. Vincent Aerobiology over Antarctica – A new initiative for atmospheric ecology Frontiers in Microbiology, 7 doi: 10.3389/fmicb.2016.00016

M. Plissonneau, J. Pansieri, L. Heinrich-Balard, JF Morfin, N. Stransky-Heilkron, P. Rivory, P. Mowat, M. Dumoulin, R. Cohen, E. Allemann, E. Toth, MJ Saraiva, C. Louis, O. Tillement, V. Forge, F. Lux and C. Marquette Gd-nanoparticles functionalization with specific peptides for beta-amyloid plaques targeting J. Nanobiotechnol., DOI 10.1186/s12951-016-0212-y

F. Roulling, A. Godin, A. Cipolla, T. Collins, K. Miyazaki and G. Feller Activity-stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures Extremophiles, 20, 621-629 JF Simon, A. Bouillez, JM Frère, A. Luxen and A. Zervosen Synthesis of an enantiopure thioester as key substrate for screening the sensitivity of penicillin binding proteins to inhibitors ARKIVOC, 22-31

N. Stankovic, M. Schloesser, M. Joris, E. Sauvage, M. Hanikenne and P. Motte Dynamic distribution and interaction of the Arabidopsis SRSF1 subfamily splicing factors Plant Physiol, 170, 1000-1013

I. Stelmach Pessi, P. De Carvalho Maalouf, H.D. Laughinghouse IV, D. Baurain and A. Wilmotte On the use of high-throughput sequencing for the study of cyanobacterial diversity in Antarctic aquatic mats J. Physiol., 52, 356-368

M. Urem, T. van Rossum, G. Bucca, GF Moolenaar, E. Laing, M. A. Swiatek-Polatynska, J. Willemse, E. Tenconi, S. Rigali, N. Goosen, C.P. Smith and G.P. van Wezel OsdR of Streptomyces coelicolor and the dormancy regulator DevR of Mycobacterium

tuberculosis control overlapping regulon mSystems, 1, e00014-16


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REVIEWS J.M. Frère and S. Rigali The alarming increase in antibiotic-resistant bacteria Drug Target Review, 3, 26-30 E. Sauvage and M. Terrak Glycosyltransferases and transpeptidases/penicillin-binding proteins: valuable targets for new antibacterials Antibiotics, 5, 12; doi:10.3390/antibiotics5010012 M. Urem, MA Swiatek-Polatynska, S. Rigali and GP van Wezel Intertwining nutrient-sensory networks and the control of antibiotic production in Streptomyces Mol. Microbiol., 102, 183-195


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PUBLICATIONS 2017 M. Barroca, G. Santos, B. Johansson, F. Gillotin, G. Feller and T. Collins Deciphering the factors defining the pH-dependence of a commercial glycoside hydrolase family 8 enzyme Enzyme Microb. Technol., 96, 163-169

A. Chevigné, V. Campisi, M. Szpakowska, D. Bourry, M.-E. Dumez, JC Martins, A. Matagne, M. Galleni and A. Jacquet The Lys-Asp-Tyr triad within the mite allergen Der p1 propeptide is a critical structural element for the pH-dependent initiation of the protease maturation Int. J. Mol. Sci., 18, 1087, doi:10.3390/ijms18051087 O. Crasson, G. Courtade, RR Léonard, FL Aachmann, F. Legrand, R. Parente, D. Baurain, M. Galleni, M. Sørlie and M. Vandevenne Human chitotriosidase: catalytic domain or carbohydrate binding module, who’s leading HCHT’s biological function Scientific Reports/7:2768/DOI:10.1038/s41598-017-02382-z J. Dagnino-Leone, M. Figueroa, C. Mella, M.A. Vorphal, F. Kerff, A.J. Vásquez, M. Brunster and J. Martínez-Oyanedel Structural models of the different trimers present in the core of the phycobilisomes from Gracilaria chilensis based on crystal structures and sequences PLOS ONE/https://doi.org/10.1371/journal.pone.0177540 J. De Meutter, J. Vandenameele, A. Matagne and E. Goormaghtigh Infrared imaging of high density protein arrays Analyst, 142, 1371-1380

S. Di Gregorio, S. Fernandez, A. Cuirolo, O. Verlaine, A. Amoroso, D. Mengin-Lecreulx, A. Famiglietti, B. Joris and M. Mollerach Different vancomycin-intermediate Staphylococcus aureus phenothpes selected from the same ST100-hVISA parental strain Microb. Drug Resist, 23, 44-50, DOI:10.1089/mdr.2016.0160 M. El Ghachi, N. Howe, R. Auger, A. Lambion, A. Guiseppi, F. Delbrassine, G. Manat, S. Roure, S. Peslier, E. Sauvage, L. Vogeley, J.-C. Rengifo-Gonzalez, P. Charlier, D. Mengin-Lecreulx, M. Fogllino, T. Touzé, M. Caffrey and F. Kerff Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis Cell. Mol. Life Sci., 74, 2319-2332 C. Fagliarone, C. Mosca, I. Ubaldi, C. Verseux, M. Baqué, A. Wilmotte and D. Billi Avoidance of protein oxidation correlates with the desiccation and radiation resistance of hot and cold desert strains of the cyanobacterium Chroococcidiopsis Extremophiles, 21, 981-991


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A. Frère, A. Baroni, E. Hendrick, A.-S. Delvigne, F. Orange, O. Peulen, G.R. Dakwar, J. Diricq, P. Dubois, B. Evrard, K. Remaut, K. Braeckmans, S. C. De Smedt, J. Laloy, J.-M. Dogné, G. Feller, L. Mespouille, D. Mottet and G. Piel PEGylated and functionalized aliphatic polycarbonate polypex nanoparticles for intravenous administration of HDAC5 siRNA in cancer therapy ACS Appl Mater Interfaces, 9, 2181-2195

J. Gubbens, C. Wu, H. Zhu, D. V. Filippov, B. I. Florea, S. Rigali, H. S. Overkleeft and G.P. van Wezel Intertwined precursor supplu during biosynthesis of the catecholate-hydroxamate siderophores qinichelins in Streptomyces sp. MBT76 ACS Chem. Biol., 12, 2756-2766 A. Jacquet, V. Campisi, M. Szpakowska, M.-E. Dumez, M. Galleni and A. Chevigné Profiling the extended cleavage specificity of the house dust mite protease allergens Der p1, Der p3 and Der p6 for the prediction of new cell surface protein substrates Int. J. Mol. Sci., 18, 1373, doi:10.3390/ijms18071373 S. Jourdan, I.M. Francis, B. Deflandre, R. Loria and S. Rigali Tracking the subtle mutations driving host sensing by the plant pathogen Streptomyces scabies mSphere, e00367-16

J. Kleintech, S. Golubic, I. S. Pessi, D. Velazquez, J-Y Storme, F. Darchambeau, A. V. Borges, P. Compère, G. Radtke, S-J Lee, E.J. Javaux and A. Wilmotte Cyanobacterial contribution to travertine deposition in the Hoyoux river system, Belgium (+ supplements) Microbiol. Ecol., 74, 33-53 Y. Lara, B. Durieu, L. Cornet, O. Verlaine, R. Rippka, I. S. Spessi, A. Misztak, B. Joris, E. J. Javaux, D. Baurain and A. Wilmotte Draft genome sequence of the axenic strain Phormidesmis priestleyi ULC007, a cyanobacterium isolated from Lake Bruehwiler (Larsemann Hills, Antarctica) Genome Announc, 5, e01546-16 S. Leclercq, A. Derouaux, S. Olatunji, C. Fraipont, A.J.F. Egan, W. Vollmer, E. Breukink and M. Terrak Interplay between penicillin-binding proteins and SEDS proteins promotes bacterial cell wall synthesis Scientific Reports, DOI: 10.1038/srep43306

M. Maciejewska, D. Adam, A. Naômé, L. Martinet, E. Tenconi, M. Calusinska, P. Delfosse, M. Hanikenne, D. Baurain, P. Compère, M. Carnol, H.A. Barton and S. Rigali Assessment of the potential role of Streptomyces in cave moonmilk formation Frontiers in Microbiology, doi: 10.3389/fmicb.2017.01181 A. Matagne, L. Bolle, R. El Mahyaoui, D. Baeyens-Voland and M. Azarkan The proteolytic system of pineapple stems revisited: purification and characterization of multiple catalytically active forms Phytochemistry, 138, 29-51


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J. Pansieri, M. Plissonneau, N. Stransky-Heilkron, M. Dumoulin, L. Heinrich-Balard, P. Rivory, JF Morfin, E. Toth, MJ Saraiva, E. Alléman, O. Tillement, v. Forge, F. Lux and C. Marquette Multimodal imaging Gd-nanoparticles functionalized with Pittsburgh compound B or a nanobody for amyloid plaques targeting Nanomedicine, 12, 1675-1687 B. Ramalapa, O. Crasson, M. Vandevenne, A. Gibaud, E. Garcion, T. Cordonnier, M. Galleni and F. Boury Protein-polysaccharide complexes for enhanced protein delivery in hyaluronic acid templated calcium carbonate microparticles J. Mater. Chem. B, 5, 7360-7368 M.M. Rodriguez, R. Herman, B. Ghiglione, F. Kerff, G. D’Amico Gonzalez, F. Bouillenne, M. Galleni, J. Handelsman, P. Charlier, G. Gutkind, E. Sauvage and P. Power Crystal structure and kinetic analysis of the class B3 di-zinc metallo-beta-lactamase LRA-12 from an Alaskan soil metagenome PLOS ONE/https://doi.org/10.1371/journal.pone.0182043 M. Ruggiero, L. Curto, F. Brunetti, E. Sauvage, M. Galleni, P. Power and G. Gutkind Impact of mutations at Arg220 and Thr237 in PER-2 beta-lactamase on conformation, activity, and susceptibility to inhibitors Antimicrob Agents Chemother, 61, e02193-16 K.N. Sathish Yadav, H.V. Miranda-Astudillo, L. Colina-Tenorio, F. Bouillenne, H. Degand, P. Morsomme, D. González-Halphen, E.J. Boekema and P. Cardol Atypical composition and structure of the mitochondrial dimeric ATP synthase from Euglena

gracilis Biochim. Biophys. Acta, 1858, 267-275 L. Sevaille, L. Gavara, C. Bebrone, F. de Luca, L. Nauton, M. Achard, P. Mercuri, S. Tanfoni, L. Borgianni, C. Guyon, P. Lonjon, G. Turan-Zitouni, J. Dzieciolowski, K. Becker, L. Bénard, C. Condon, L. Maillard, J. Martinez, JM Frère, O. Dideberg, M. Galleni, JD Docquier ane JF Hernandez 1,2,4-triazole-3-thione compounds as inhibitors of dizinc metallo-beta-lactamase Chem. Med. Chem, 12, 972-985 D. Thorn, J. Kay, N. Rhazi, M. Dumoulin, A. Corazzo and C. Damblon 1H,13C and 15N backbone resonance assignments of the beta-lactamase BlaP from Bacillus

licheniformis 749/C and two mutational variants Biomol NMR Assign, DOI 10.1007/s12104-017-9782-3 R. Van Assche, C. Borghgraef, J. Vaneyck, M. Dumoulin, L. Schoofs and L. Temmerman In vitro aggregating beta-lactamase-polyQ chimeras do not induce toxic effects in a in vivo Caenorhabditis elegans model J. Negat Results Biomed, 16, DOI 10.1186/s12952-017-0080-5


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REVIEWS G. Feller Cryospher and psychrophiles: insights into a cold origin of life Life, 7, 25; doi:10.3390/life7020025 R. Kurmayer, K. Sivonen, A. Wilmottte and N. Salmaso (Editors) Molecular tools for the detection and quantification of toxigenic cyanobacteria Wiley, ISBN: 978-1-119-33210-7 M. A. Furmaniak, A. E. Misztak, M. D. Franczuk, A. Wilmotte, M. Waleron and K. F. Waleron Edible cyanobacterial genus Arthrospira: actual state of the art in cultivation methods, genetics and application in medicine Front. Microbiol., 8:2541.doi:10.3389/fmicb.2017.02541


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PROTEIN STRUCTURES DEPOSITED WITHIN THE PROTEIN DATA BANK

PDB ID STRUCTURE TITLE AUTHOR

5JKI

CRYSTAL STRUCTURE OF THE FIRST TRANSMEMBRANE PAP2 TYPE

PHOSPHATIDYLGLYCEROLPHOSPHATE PHOSPHATASE FROM

BACILLUS SUBTILIS

El Ghachi, M., Howe, N., Lampion, A., Delbrassine, F., Vogeley, L., Caffrey, M., Sauvage, E., Auger, R., Guiseppe, A., Roure, S., Perlier, S., Mengin-lecreulx, D., Foglino, M., Touze, T.

5HJL CRYSTAL STRUCTURE OF CLASS I TAGATOSE 1,6-BISPHOSPHATE

ALDOLASE LACD FROM STREPTOCOCCUS PORCINUS Freichels, R., Kerff, F., Herman, R., Charlier, P., Galleni, M.

5LYA STRUCTURE OF THE W64R AMYLOIDOGENIC VARIANT OF HUMAN

LYSOZYME

Vettore, N., Herman, R., Kerff, F., Charlier, P., Sauvage, E., Brans, A., Morray, J., Dobson, C., Kumita, J., Dumoulin, M.

5LWF

STRUCTURE OF A SINGLE DOMAIN CAMELID ANTIBODY FRAGMENT

CAB-G10S IN COMPLEX WITH THE BLAP BETA-LACTAMASE FROM

BACILLUS LICHENIFORMIS

Vettore, N., Kerff, F., Pain, C., Herman, R., Sauvage, E., Preumont, S., Charlier, P., Dumoulin, M.

5TJF THE CRYSTAL STRUCTURE OF ALLOPHYCOCYANIN FROM HE RED

ALGAE GRACILARIA CHILENSIS

Figueroa, M., Dagnino, J., Kerff, F., Charlier, P., Bunster, M., Martinez-Oyanedel, J.

5OON STRUCTURE OF UNDECAPRENYL-PYROPHOSPHATE PHOSPHATASE, BACA

El Ghachi, M., Howe, N., Huang, C.Y., Olieric, V., Warshamanage, R., Touze, T., Weichert, D., Stansfeld, P.J., Wang, M., Kerff, F., Caffrey, M.


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SYMPOSIA 2016 Belgian National Committee for Geodesy and Geophysics (BNCGG) – Belgian National Committee on Antarctic Research (BNCAR) 2016 Symposium, Royal Academy of Sciences, Brussels, Belgium, April 29 Main organizers: A. Wilmotte, F.Pattyn and T. Camelbeeck WORKSHOP - Advances in cryopreservation methods for microorganisms and plants, Berlin, Germany, June 21 Main organizers: A. Wilmotte, C. Crahay and W. Vyverman (UGent) Mini-symposium MS 3. Linking Antarctic science with environmental protection: Celebrating the 25th anniversary of the Madrid Protocol, Kuala Lumpur, Malaysia, August 23 Main organizers: A. Wilmotte, J. Xavier (Portugal), K. Hughes (United Kingdom), G. Roldan (Argentina), J. Lopez-Martinez (Spain) Fourteenth Meeting of the Belgian Biophysical Society on “Protein Folding and Stability”, University of Liège, Belgium, September 2 Main organizer: Prof. A. Matagne Third BIBR (Belgian Interdisciplinary Biofilm Research) meeting, University of Liège, Belgium. September 8 Main organizers: Dr C. Duez and J. Mahillon (UCL) 27th Faltertage on “Protein Folding, Dynamics and Stability, Melanchthonianum, Martin-Luther University Halle-Wittenberg, Halle, Germany, October 21-23 Chair: Prof. Matagne The Bioforum of BioLiège, University of Liège, Belgium, November 16 Main organizers: Prof. J. Dommes, Prof. B. Joris, T. Dauvrin (BioLiège association) Mini-Symposium on Microcalorimetry of biological macromolecules, Université de Liège, Belgium, November 22

Main organizer: Prof. A. Matagne


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SYMPOSIA 2017 Workshop on “Challenges and Opportuities in Protein Analytics”, orgnanized by the F.R.S.-FNRS Graduate School SFMBBM and the Belgian Biophysical Society, ULB Campus La Plaine, Brussels, Belgium, March 10 Co-organizer and chair: Prof. A. Matagne SCAR Biology 2017 Symposium – Session S10 'Understanding physiology (including '-omics' approaches), Leuven, Belgium, July 10-13 Co-organizer: Dr A. Wilmotte 19th IUPAB Congres and 11th EBSA Congress, Edinburgh, United Kingdom, July 16-20 Co-organizer and co-chair: Prof. A. Matagne (both with Jane Clarke) of the session on Protein Folding, Assembly and Stability EBSA 2017 Satellite Meeting - Biophysical Approaches to Protein Folding and Disease, Edinburgh, United Kingdom, July 20-21 Co-organizer and Co-chair: Prof. A. Matagne with Mauro Dalla Serra (Italy), Rob Gilbert (UK), and Patrick England (France)

Fifteenth Meeting of the Belgian Biophysical Society on “Protein Folding and Stability”, University of Liège, Belgium, September 1 Main organizer: Prof. A. Matagne 1st one-day symposium on Current trends in membrane protein biophyics, Univresity of Namur, Belgium, December 1 Co-organizer (scientific and organizing board) and chair: Prof. A. Matagne

EDUCATION

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ACADEMIC COURSES

Bachelor and Preparation to Masters

Biochimie, 30 h - CHIM0678-1 - A. Matagne

Bac3 Sciences chimiques et année préparatoire aux Sciences Chimiques Biochimie et thermodynamique des systèmes biologiques, 40h + 20h Pr - BIOC0204-1 - M. Galleni Bac 2 Sciences biologiques Biologie et introduction à la biochimie, 30h + 30h Pr - BIOL2009-1 - B. Joris

Bac 2 Sciences Chimiques Biophysique et biochimie, 30h Th, 24h Pr, 6h Proj- GBIO0001-1 – P. Charlier, L. Geris Bachelier en sciences de l'ingénieur, orientation ingénieur civil Chimie des macromolécules biologiques, 60h + 40h Pr + 4h de visite d’usine - BIOC0209-3/4/6 - M. Galleni et A. Matagne

Bac 3 Sciences biologiques et année préparatoire aux masters en Biochimie et Biologie Moléculaire et Cellulaire (BBMC) et Biologie des Organismes et Ecologie (BOE) Chimie des macromolécules biologiques etthermodynamique des systèmes biologiques, 70h + 40h Pr + 4h de visite d’usine - BIOC0209-4 - M. Galleni et A. Matagne

Année préparatoire aux masters en sciences biologiques Génétique, biologie moléculaire et chimie des macromolécules, 30h + 30h Pr - BIOC0001-1 J. Dommes et M. Galleni. Bac 3 Sciences biologiques et année préparatoire au master BOE Microbiologie - MICR0711-1 Partim 2 : Bactériologie : 20h + 10h Pr – B. Joris Bac 3 et années préparatoires aux masters BBMC et BOE

Masters

Analyse des séquences des gènes et des protéines : partim a, 10h, 10h Pr - GBIO0007-1 - B. Joris

Master 2 en Bioinformatique et modélisation, finalité approfondie et master 2 en Ingénieur civil biomédical, finalité approfondie Application des techniques spectroscopiques à l’étude du repliement et de la stabilité des protéines, 20h+10h TD - BIOC0722 – A. Matagne Aspects génétiques et biochimiques de l'évolution, 25h + 20h Pr - GENE0432-3 - M. Galleni

et C. Remacle. Masters 1 BBMC et BOE Astrobiologie, 30h Th. – GEOL0263-2 – Ph. Claeys, Véronique Dehant, M. Galleni, E. Javaux, Y. Nazé et A. Wilmotte. Master 2 en Biologie des Organismes et Ecologie, à finalité approfondie

Biochimie, 30 h + 40 h Pr - BIOC0002-2 - P. Charlier

Master 1 en Bioinformatique et modélisation, finalité approfondie Biochimie et physiologie des microorganismes, 20h + 20h Pr - BIOC0003-2 - B. Joris

Masters 1 BBMC et BOE

EDUCATION

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Biochimie macromoléculaire, 30h + 30h Pr - BIOC0232-1- M. Galleni - Master 1 Sciences chimiques Bioinformatique appliquée, 10h Th + 10h Pr - BIOC0717-2 - B. Joris - Master 2 BBMC Biophysique et biochimie, 30h Th, 24h Pr, 6h Proj- GBIO0001-1 – P. Charlier, L. Geris Master en ingénieur civil biomédical, à finalité Chimie des macromolécules biologiques, 60h + 40h Pr + 4h de visite d’usine - BIOC0209-3/4 M. Galleni et A. Matagne - Master générique en Sciences biologiques Compléments de microbiologie : pathogénicité bactérienne, 15h Th - MICR0004-1 - B. Joris Master 1 BBMC Développement des microorganismes, 15h Th. BIOL0013-1 – S. Rigali - Master 1 BBMC Enzymologie, 15h - BIOC0719-1 - A. Matagne - Master 1 Sciences chimiques Enzymologie, 15h + 25h Pr - BIOC0719-2 - A. Matagne - Master 1 Bioinformatique et modélisation Functional and Molecular Marine Microbiology, Molecular approaches to the diversity of marine microorganisms, 15h + 15h Pr. - OCEA0064-4 – A. Wilmotte - Master 2 en Océanographie à finalité approfondie Interactions dans les macromolécules biologiques, 20h + 20h Pr – BIOC0712-1 - M. Galleni - Master 1 Bioinformatique et modélisation, finalité approfondie

Introduction to systems and synthetic biology, 30h Th + 30h Pr - GBIO0016-1-a - B. Joris - Master 2 en Bioinformatique et modélisation Introduction to synthetic biology. 10h Th + 20h Pr - GBIO0019-1-a - B. Joris et F. Delvigne - Master 2 en Bioinformatique et modélisation Microorganismes extremophiles, 25h Th – MICR01713-1 - G. Feller, M. Galleni et A. Wilmotte

Master1 BBMC Advance concepts on protein structure-function relationships, 2h - SBIM0495-1- M. Dumoulin -

Master 2 Sciences Biomédicales Multidisciplinary English Molecular and cellular basis of disease: Protein misfolding and aggregation diseases, generalities, 1 h - SBIM0495-1 - M. Dumoulin - Master 2 Sciences Biomédicales Multidisciplinary English New therapeutic approaches to disease: Various uses of Nanobodies in diagnosis and treatment, 2 h - SBIM0497-1 - M. Dumoulin - Master 2 Sciences Biomédicales Multidisciplinary English Propriétés fonctionnelles des macromolécules biologiques, 20h+10h TD+ 20h Pr - BIOC0210-5 A. Matagne - Master 1 BBMC et Sciences Biologiques Propriétés optiques des macromolécules biologiques, 15h + 20h Pr. BIOC0721-A – C. Damblon et A. Matagne - Master 1 BBMC et BOE Relations structure-fonction dans les biomolécules, 15h + 25h Pr - BIOC0718-2 – M. Dumoulin Master 2 Ingénieur civil biomédical, finalité approfondie

EDUCATION

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Structural biological chemistry, 30h Th – CHIM0650-1 – C. Damblon & A. Matagne (lecture on the application of spectroscopic methods to protein studies at the molecular level, 2h) – Master en sciences chimiques, à finalité Structure des macromolécules biologiques, 15h Th, 5h TD - BIOC0720-2 – P. Charlier - Master en sciences biomédicales, à finalité, Master en biochimie et biologie moléculaire et cellulaire, à finalité Structure des macromolécules biologiques, (aspects expérimentaux généraux) : partim a 20h + 10h Pr - CHIM0624-1 - P. Charlier, C. Damblon, E. De Pauw - Master 2 Bioinformatique et modélisation, finalité approfondie Structure des macromolécules biologiques, (aspects expérimentaux) : partim b1 (RX, RMN), 15h + 10h Pr - CHIM0627-1 - P. Charlier, C. Damblon - Master 2 Bioinformatique et modélisation, finalité approfondie

Inter University Thematic Weeks

Antibiotic resistance, 25h + 25 Pr – BIOC0716-1 - M. Galleni, F. Kerff, M. Terrak et JM Frère - Master 2 BBMC Microorganismes extrémophiles, 25h + 25h Pr - MICR0713-1 - M. Galleni, G. Feller et A. Wilmotte

Master 2 BBMC. Structure et fonction des protéines, 25h + 25h Pr - BIOC0715-1 - P. Charlier et M. Dumoulin

Master 2 BBMC, finalités approfondie, didactique et industrielle Visualisation et modélisation des protéines. 25h Th + 25h Pr - BIOC9239-1 – P. Charlier, F. Kerff et E. Sauvage - Master 2 BBMC

Complementary Masters

Structure des macromolécules biologiques, 15h Th, 20h Pr, 5h TD - BIOC0720-1 - P. Charlier Master de spécialisation en nanotechnologie Chimie des macromolécules biologiques, 20h - BIOC0209-3/4/6 - M. Galleni et A. Matagne

Master complémentaire en Nanotechnologie Génie génétique des bactéries, 15h – GENE2000-1 - A. Brans - Master complémentaire en Biotechnologie et Biologie appliquée Microbiologie - MICR0711-1 Partim 2 : Bactériologie : 20h + 10h Pr – B. Joris - Master complémentaire en Biotechnologie et Biologie appliquée

Propriétés fonctionnelles des macromolécules biologiques, 20h+10h TD+ 20h Pr - BIOC0210-5 A. Matagne - Master complémentaire en Nanotechnologie

Third Cycle

Advanced course on « Protein purification: What to do and how » - 15h - SDOC0048-1 - E. Depauw, J.-M. Frère, M. Galleni, B. Joris et A. Matagne, 2016 and 2017

EDUCATION

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Courses given abroad

Bioinformatique, 35 h - A. Brans – Licence Pro Génie biologique - IUT de Mont de Marsan, Université de Pau et des Pays de l’Adour, France, Octobre 2016 Production de protéines recombinantes, 10 h - M. Delmarcelle - Licence Pro Génie biologique - IUT de Mont de Marsan, Université de Pau et des Pays de l’Adour, France, Octobre 2016 Nanobodies or camelid antibody fragments: Properties and application; Protein folding and stability; Advanced concepts on protein structure and function, 8 h – M. Dumoulin Department of Pharmaceutical Sciences, University of Padova, Italy, November 28 – December 1, 2016 Enzyme kinetics, Protein folding and Protein Purification - J.-M. Frère, M. Vandevenne and

M. Dondelinger, Masters en Biotechnologie et Microbiologie. Cycle de 3 ans, 15h/an. Università degli Studi di Siena, Siena, Italy

Courses during the Summer School for PhD students “Floraciones Algales en Aguas Continentales:

Aspectos taxonómicos, moleculares, ecológicos, paleolimnológicos y sus implicancias para la salud de

la población” – A. Wilmotte, University of Conception, Chili, January 9-13, 2017

Postgraduate Erasmus course on “Optical spectroscopy to characterize protein conformation and

conformational changes” – A. Matagne, Università degli Studi di Siena, Siena, Italy, June 12-15,

2017

Enzyme kinetics – J.-M. Frère - Università degli Studi di Siena, Siena, Italy, June 12-15 2017 Nanobodies or camelid antibody fragments: Properties and application; Protein folding and stability; Advanced concepts on protein structure and function, 8 h – M. Dumoulin Department of Pharmaceutical Sciences, University of Padova, Italy, November 28 – December 1, 2017

Courses given in another Belgian university

Circular Dichroism applied to protein studies, 2 h, as part of “Protein Biophysics and Engineering” – A. Matagne, Master 1 in Chemistry, University of Namur (FUNDP), Namur, March 1, 2016 and March 1, 2017

Training for scientists Training on preservation of microorganisms, isolation and cultivation, morphological and molecular

characterization of cyanobacteria – BCCM training - A. Wilmotte & K. Beets

September 19-22, 2017

EDUCATION

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TRAINEES AND STUDENTS

Master I Trainees – 2016 BERTHOL Pierre-Marie BLETARD Sylvie COLLIGNON Alice CORNET Jordan DEHAYE Jordan DEVAUX Delphine GERDAY Sara GOUASMIA Houda HABETS Audrey HULIN Julie JACOB Nathan LA ROCCA Raphaël SICILIANI Justine THISSEN Romain VO Sarah ZWAENEPOEL Manon

Master I Trainees – 2017

BONOMETTI Beatrice DELBROUCK Timothé FOUILLEN Nicolas JORSSEN Joseph LENAERTS Anne-Cécile LUPO Valérian MALEMPRE Romain NIX Benoit PIERRE Jonas TRIGALLEZ Sarah WATERPLAS Dries

Master II Students - 2016

ADAM Delphine Master II BBMC à finalité approfondie, ULg Evaluation des activités antimicrobiennes et du rôle présumé de

souches de Streptomyces dans la genèse des dépôts de moonmilk BEJI Bassem Master en sciences de l’ingénieur industriel (finalité biochimie) HEPL – ISIL, Liège Etude des conditions de la stabilisation d'une phénylalanine

déshydrogénase

BOES Adrien Master II BBMC à finalité approfondie, ULg Etude des interactions et activités du noyau enzymatique du

divisome chez Escherichia coli

CHAUVEAU Claire Master II Oceanography, ULg Analysis of tetrodotoxin production in bacteria associated with

blue-lined octopuses

DEFISE Antoine Master II BBMC à finalité approfondie, ULg

Recherche et analyse des opérons codant pour les métabolites

secondaires dans les génomes des cyanobactéries

DURAY Elodie Master II BBMC à finalité approfondie, ULg Caractérisation conformationnelle des lncRNAs BC1 & RL-P4P6

et ingénierie de nanobodies dirigés contre ces ARNs

EDUCATION

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GUILBEAU Etienne Master II Ingénieur en chimie et génie des procédés CPE Lyon, France Développement de la fonctionnalisation d’une matrice nouvelle

génération à haute résolution et faible coût pour la purification de

biomolécules MICHAUX Stéphane Master II BBMC à finalité approfondie, ULg Etude de supports carbonés poreux modifiés destinés à la

séparation de biomolécules (protéines)

RAYMACKERS Alice Master II BBMC à finalité approfondie, ULg Etude de l'induction de la β-lactamase BlaP chez Bacillus

licheniformis

RENGIFO GONZALES Master II BBMC à finalité approfondie, ULg Juan Carlos Characterization of YodM mutants: a transmembrane

phosphatidylglycerol-phosphate phosphatase involveld in

phospholipid metabolism in Bacillus subtilis

ROBERT Charly Master II BBMC à finalité approfondie, ULg Production, purification and kinetic study of laboratory mutants

Q123 of NDM-1 metallo-β-lactamase

WETZELS Loïc Master II BBMC à finalité approfondie, ULg

Etude du PBP5 d'Enterococcus faecium

Master II Students – 2017 ANDERSSEN Sinaeda Master II BBMC à finalité approfondie, ULg

Unveiling signallling pathways from plant material to the onset of

secondary metabolism in Actinobacteria BLETARD Sylvie Master II BBMC à finalité approfondie, ULg

Etude de la metallo-beta-lactamase de sous-classe B2 YEM-1

produite par Yersinia mollaretti Wauters

CAWEZ Frédéric Master II BBMC à finalité approfondie, ULg

Ingénierie de fragments d'anticorps de camélidés (nanobodies)

capables de reconnaître des ARNs structurés DAUVRIN Thomas Master II en bioingénieur : chimie et bioindustries, à finalité

spécialisée, Gembloux, ULg Caractérisation de composés bioactifs issus de l’espèce

Phormidesmis priestleyi

DEFLANDRE Benoît Master II BBMC à finalité approfondie, ULg

Etude des mécanismes d'induction de la pathogénicité chez

Streptomyces scabies DEVAUX Delphine Analytical platform GRS Enzym. Puratos N.V.

New Enzymes discovery & customer enzymes.

EDUCATION

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VANEYCK Jonathan Master II BBMC à finalité approfondie, ULg

Use of structural probes for the study of the mechanism of

aggregation of alpha-synuclein into amyloid fibrils

Erasmus students – 2016

DI COSTANZO Stefano Master II, Faculty of Molecular and Industrial Biotechnology University of L’Aquila, Italy The role of non-catalytic residues in the thermostability of

BlaZ enzyme

GENCO Alessandro MSc in Biology, University of Pisa, Italy

Production of artificial proteins known as “Octarellins”

GIRAUDON Maylis Diplôme Universitaire et Technologique de Génie Biologique, Université de Pau et des Pays de l’Adour, France Clonage, production, purification et analyse de proteins

homologues à la protéine BlaR-CTD de Bacillus licheniformis 749i

MASTROSANTI Master II, University of Rome, Tor Vergata Gian Marco Structural and functional characterization of the C-terminal

domain of the A TPase HMA4 involved in metal

hyperaccumulation in Arabidopsis halleri

MILLARET Thomas Licence professionnelle en biotechnologie, Université de Pau et des Pays de l’Adour, France

Construction, production et purification de variantes de la GFP

pour servir le développement d'un système microfluidique

d'électrophorèse en écoulement libre

NASTRO Ariana Master II, Faculty of Molecular and Industrial Biotechnology,

Unversity degli Studi di Napoli “Federico II”, Italy Functional and structural characterization of the Arabidopsis

halleri HMA4 C-terminal domain

NAUDI Samuel Diplôme Universitaire et Technologique de Génie Biologique Université de Pau et des Pays de l’Adour, France

Conception, production et purification de différentes GFP en vue

de la caractérisation de récepteurs

PISANO Agnese Master II, Faculty of Molecular and Industrial Biotechnology,

Unversity degli Studi di Napoli “Federico II”, Italy Heterologous expression and purification of the human RMB10

and the Arabidopsis ABI3-5 suppressor zinc finger

ROUSSIN Clément Licence professionnelle en biotechnologie, Université de Pau et des Pays de l’Adour, France Clonage, production et purification d'une protéine recombinante

"VIM-2"

EDUCATION

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VETTORE Nicola Master II, Faculty of Pharmacy, University of Padova, Italy Biophysical characterization of the W64R amyloidogenic variant

of human lysozyme

Erasmus students – 2017 BROSSEAU Natan Licence professionnelle en biotechnologie Université de Pau et des Pays de l’Adour, France

Construction, production et purification de deux GFP pour le

développement d’un système de purification : le système

microfluidique d’électrophorèse en écoulement libre (µFFE)

BRUDER Adrien Ingénieur en génie des procédés et bioprocédés Université de Nantes, France Utilisation de systèmes aqueux à deux phases pour la purification

de protéines

CANTEGRIL Alexandra DUT génie biologique option Industries Agroalimentaires

Université de Pau et des Pays de l’Adour, France Mutagenese, clonage, expression et production de Blar-CTD de

Bacillus licheniformis 749i dans Bacillus subtilis 168 et Bacillus

subtilis WB800N

LABARTHE Flavie Licence professionnelle en biotechnologie

Université de Pau et des Pays de l’Adour, France Clonage, production et purification de birA LAPEYRE Amélie Diplôme Universitaire et Technologique de Génie Biologique

Université de Pau et des Pays de l’Adour, France Etude de l’induction de la beta-lactamase BlaB chez Bacillus

licheniformis

MAROTO Claudia Master II, Universidad Politécnica de Madrid, Spain Production of selected Octarellin variants

NGOUALA Oren Licence professionnelle en biotechnologie

Université de Pau et des Pays de l’Adour, France Clonage et production dans Bacillus subtilis 168 de protéines liant

la pénicilline

RAMALAPA Bathabile Université d’Angers, France

Design of new delivery systems for therapeutic proteins based on

calcium carbonate microspheres

SILVESTRI Mauro Master II, Faculty of Molecular and Industrial Biotechnology

Unversity degli Studi di Napoli “Federico II”, Italy Studi of the outer membrane permeability of Pseudomonas

aeruginosa to carbapenems

TINTURIER Dimitri Licence professionnelle en biotechnologie

Université de Pau et des Pays de l’Adour, France Construction, production et purification de variants de la GFP

pour explorer la reconnaissance de récepteurs auto-assembés

EDUCATION

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Technical high schools – Bachelor III – 2016

BEGASSE Brice Master en sciences de l’ingénieur industriel, finalité biochimie HEPL – ISIL, Liège Développement et validation expérimentale d'un logiciel intégré

de contrôle et d'analyse de purification de protéines par

électrophorèse en puce microfluidique et modélisation de ses

paramètres principaux

DUMOULIN Marine Bachelier – Technologue de laboratoire

HELMO Sainte-Julienne, Liège Clonage, production, purification et analyse de protéines

homologues à la Protéine BlaR-CTD de Bacillus licheniformis 749i

FELLER Tom Bachelier en Biochimie HEPL – ISIL, Liège Etude de la localisation de l’amidase AmiC d’E. coli via son

domaine Amin

FRESON Pierre Technologue de laboratoire médical

Haute école de la province de Liège, André Vésale (Barbou) Développement d’un protocole d’extraction d’ADN de

cyanobactéries

MIGDALSKI Julie Bachelier-Technologue de laboratoire médical

HE Charlemagne, Liège Caractérisation de souches de cyanobactéries

Technical high schools – Bachelor III – 2017 FOSSION Apolline Bachelier – Technologue de laboratoire médical HELMO Sainte-Julienne, Liège Clonage, production, purification et analyse de la protéine

Thiamine pyrophosphokinase

GRITTEN Caroline Bachelier – Technologue de laboratoire médical HELMO Sainte-Julienne, Liège Contribution à la mise au point d’une méthode de détection de

Staphylococcus aureus, utilisant des billes magnétiques

fonctionnalisées

MINGUET Brice Bachelier – Technologue de laboratoire médical

HELMO Saint-Laurent, Liège Clonage, production et purification de protéines homologues à

BlaR-CTD dans Bacillus subtilis WB800N et B168

EDUCATION

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GENERAL PUBLIC ACTIVITIES

Activities for students of secondary schools Accueil des Rhétoriciens au CIP, par M. Boulanger, S. Fanara, J. Kay, F. Kerff, S. Leclercq, G.

Lekeux et A. Wilmotte : De la bactérie « usine à protéines » à la protéine utile à l’usine February 2, 2016 Atelier pour l’enseignement secondaire : A. Wilmotte, F. Kerff, S. Leclercq, M. Boulanger,

S. Fanara, G. Lekeux, S. Leimanis, A. Boes, M. Dauvin, J. Kay et J. Vandenameele : De la

bactérie «usine à protéines » à la protéine utile à l’usine, January 31, 2017

B. Durieu & V. Savaglia: organization of an APECS-BELSPO contest of Antarctic stories for 5th and 6th primary school and 1st secondary school, 2017 : (http://rejouisciences.uliege.be/activites/concours/concours-antarctique/) K. Beets, B. Durieu & A. Wilmotte, Institut de Chimie, ULiège, atelier pratique sur les pigments de

cyanobactéries pour la retraite scientifique de la 4ème secondaire de l’école Saint-Roch de Theux,

Belgique, March 31, 2017

B. Durieu: Regular posts on the website of APECS Belgium (Association of Polar Early Carreer

Scientists: popular Science, data tutorial, etc. in 2017

(https://apecsbelgium.wordpress.com/category/data-tutorials/)

A. Wilmotte, Atrium Covent Garden, Brussels, Presentation of research projects at the « Closing

event » of an exhibition of pictures of Antarctica “Sentinels of the extreme”, September 7, 2017

B. Durieu & V. Savaglia: projection of the movie “Antarctica, sur les traces de l'Empereur”,

interview of the film-maker and debate at the University of Liège, September 27, 2017

(https://www.facebook.com/events/480535182315165/)

B. Durieu & V. Savaglia: for the Antarctica day, creation and publication of the “Maps of Belgian polar research and expedition in 2017/2018”, November 26, 2017 (https://apecsbelgium.wordpress.com/maps-of-belgian-polar-research/belgian-polar-expeditions/

EDUCATION

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WIDE AUDIENCE CONFERENCES

Dr A. Wilmotte, « Le traité sur l’Antarctique, une gouvernance originale pour un continent exceptionnel », Cours Espace Universitaire, Liège, February 18, 2016 Dr A. Wilmotte, « S’adapter pour survivre : la biodiversité terrestre antarctique», Cours Espace Universitaire, Liège, March 3, 2016

Prof. J.-M. Frère, « Les bactéries font de la résistance – Les antibiotiques sont-ils encore efficaces ? », Espace universitaire de Liège - Conférences Sciences et Avenir 2016-2017, Cycle 3 : Médicaments ou poisons, Liège, March 16, 2017 Prof. J.-M. Frère, « Les bactéries résistantes : le retour ? », Société Royale des Sciences, Liège, November 11, 2017 Dr A. Wilmotte et V. Savaglia, «Qui vit dans les conditions extrêmes de l’Antarctique ? », Université du troisième âge, Liège, November 14, 2017

NATIONAL & INTERNATIONAL EXCHANGES

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POSTDOCS IN – 2016

I joined the CIP team in December 2016 to work on the Single C0ells project, a collaboration of industrial partners and universities supported by the Walloon region. In cooperation with Puratos, an international operating company that is specialized in the production of pastries, we are currently investigating the heterogeneity of Bacillus strains cultures during fermentation.

Already within the scope of my PhD at the University of Münster in Germany, I optimized Bacillus strains genetically with respect to their handling, biological containment and productivity, always aiming at the generation of expression platforms for the industrial production of various extracellular enzymes. As genetic accessibility constitutes a prerequisite for these manipulations, a major part of my work was focused on natural genetic competence, a bacterial state of development in which cells readily take up extracellularly supplied DNA and that can be applied as an efficient tool for transformation.

During growth, Bacillus cultures divide into different subpopulations; some cells sporulate, others produce biofilm, become motile or competent, whereas only a small part will produce the wanted enzyme. Our study will contribute to a better understanding of such cell differentiation. The introduction of a promoter-based biosensor system will make it possible to monitor heterogeneity in real time and this will enable us to react more directly to stress conditions during fermentation.

Dr Mareike Jakobs

Research group: Biological macromolecules

and biochemistry

Project leader: M. Galleni


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I joined the group of Prof. Matagne in June 2016 to establish a high-throughput screen for the optimization of protein stability/formulation at the Robotein facility. The project is part of the BEWARE program, which aims to support method transfer and development between universities and companies within the Walloon region. My fellowship is funded for 30 months of which I will spend about eight months at the company partner, Eurogentec. Before joining the CIP, I investigated the effect of chaperones on protein conformation with single-molecule fluorescence spectroscopy at the University of Zürich, where I obtained my PhD in Biochemistry. My project at the CIP aims to develop a method to test for protein stability within different buffer conditions and to investigate the effect of different additives. Besides the production and purification of different model proteins, the project includes defining the different buffer conditions and additives to be tested and further to identify and establish different methods to measure and compare the stability. The screen will help to determine the optimal conditions for protein production and storage, and therefore can help to make the production of protein based drugs cheaper but also help to simplify handling of proteins for basic research at the CIP. In a later stage, it might even be possible to deduce more general concepts on the factors that influence protein stability.

Dr Ruth Kellner

Research group: Enzymology and protein folding

Project leader : A. Matagne


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POSTDOCS IN – 2017

I have been a member of Prof. André Matagne´s Research Group, at the Centre for Protein Engineering (CIP), University of Liège, since January 2017. As a MSCA-COFUND BEWARE fellow (Marie Skłodowska-Curie Actions COFUND Programme, BEcome a WAlloon REsearcher Fellowship, co-financed by the European Union and the Walloon Region), I am carrying out my research at the interface of Academia and Industry, working at the CIP´s Robotein Platform in partnership with a Walloon company, Xpress Biologics, specialized in protein production for pre-clinical applications. The aim of my project is to develop a general method for the purification of recombinant proteins from the yeast Pichia

pastoris, which would allow rapid and efficient process and thus, might be of great economical interest for pharmaceutical and biotechnological industries. Proteins and their interactions with RNAs have always been in the heart of my research interests. I received my PhD degree in Biophysics from the Faculty of Physics, University of Warsaw, where I studied C. elegans Decapping Scavenger (DcpS) enzyme, under the supervision of Prof. Edward Darzynkiewicz. Next, I examined human DcpS inhibition by mRNA cap analogs, with Prof. Jacek Jemielity, Centre of New Technologies, University of Warsaw. My first post-doc abroad was on translation initiation on leaderless mRNAs, with Prof. Marina Rodnina, at the Max Planck Institute for Biophysical Chemistry, in Gottingen. The BEWARE Fellowship at the CIP gave me an opportunity to expand my professional experience towards high-throughput techniques of protein production, purification and analysis (capillary electrophoresis and bio-layer interferometry). In addition, I acquired industry-related professional skills, such as ability to create flow-charts and protocol templates, and to handle intellectual property data.

Dr Anna Wypijewska del Nogal

Research groupe: Enzymology and protein folding

Project leader: A. Matagne


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COLLABORATIONS ARGENTINA University of Buenos Aires – Laboratory for Bacterial Resistance – G. Gutkind, M. Mollerach &

P. Power

AUSTRALIA University of New South Wales – School of Biotechnology and Biomolecular Sciences – R. Cavicchioli & K.S. Siddiqui

AUSTRIA University of Innsbruck - Institute of Microbiology -– Austria - R. Margesin BELGIUM BCCM – Belgian Coordinated Culture Collections of Microorganisms – Brussels – M. Bosschaerts

Beldem-Puratos Group – Andenne - T. Dauvrin & J. Georis

CER Groupe – Marloie – A. Collard

E-Protein SPRl – Gembloux – J. Cornu

Euroscreen – Bruxelles – S. Blanc

FUNDP – Research Unit in Environmental and Evolutionary Biology (URBE)-Namur– P. Kestemont

FUNDP – Département de Pharmacie - Namur – B. Masereel & R. Frederik

FUNDP – Département de Chimie - Namur – C. Michaux, E. Perpète & G. Roussel

FUNDP – Laboratoire de Chimie Biologique Structurale - Namur – J. Wouters

Glaxo Smith Kline Biologicals – Rixensart – C. Gérard

Institut Scientifique de Santé Publique – Collection BCCM/IHEM – Bruxelles – M. Hendrickx KUL – Laboratory Biomolecular Dynamics – Leuven – Y. Engelborghs

KUL – Laboratory for Medicinal Chemistry – Leuven – P. Herdewijn

KUL- Functional Genomics and Proteomics Research Unit - Faculty of Sciences – Leuven - L. Schoofs & L. Temmerman

Mecasoft S.A. – Anhée – R. Brandt

National Botanical Garden of Belgium – Meise – D. Ertz & B. Van de Vyver

Nutrilab NV – Heusden-Zolder – J.M. François


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SCK-CEN – Unit of Microbiology – Mol – M. Mergeay, N. Leys & R. Van Houdt

UAntwerpen – Biomolecular and Analytical Mass Spectrometry – Antwerpen – F. Sobott &

A. Konijnenberg

UCB Pharma – Braine l’Alleud – A. Michel & E. Norrant

UCL – de Duve Institute – Bruxelles – J.F. Collet

UCL – Collection BCCM/MUCL – Louvain-la-Neuve – S. Declerck & S. Craenenbroeck

UCL - Département de Chimie – Laboratoire de Biochimie Physique et des Polymères - Louvain-la-Neuve – J. Fastrez

UCL – Earth and Life Institute – Louvain-la-Neuve – A.C. Mailleux UCL – Biochemistry and Molecular Genetics of Bacteria – Louvain-la-Neuve – P. Soumillion

UCL – Louvain Drug Resaerch Institute – Louvain-la-Neuve – R. Vanbever

UGent – Laboratory for Protein Chemistry and Biomolecular Engineering – Ghent – B. Devreese

UGent - Department of Organic Chemistry, Organic and Bioorganic synthesis - Ghent - J. Van der

Eycken UGent – Laboratory for Protistology and Aquatic Ecology – Ghent – W. Vyverman, E. Verleyen &

K. Sabbe UGent – Laboratory for Microbiology – Ghent – A. Willems & P. Vandamme

ULB – Unité de Recherche d’Immunobiologie - Laboratoire d’Allergologie Expérimentale – Gosselies – E. Adam & D. Walgraffe

ULB - Laboratoire de Bactériologie Moléculaire – Bruxelles – A. Allaoui ULB – Unité de Chimie des Protéines – Bruxelles – M. Azarkan ULB – Institut de Recherches Microbiologiques Jean-Marie Wiame – Anderlecht – C. Bauvois

ULB – Hôpital Erasme – Bruxelles – J.M. Boeynaems

ULB – Structure et Fonction des Membranes Biologiques (SFMB) - Bruxelles – E. Goormaghtigh, J.

De Meutter & V. Raussens ULB – Physiologie animale – Gosselies – M. Moser

ULB – TIP – Transfers, Interfaces and Processes – Bruxelles – B. Schneider

ULB – Laboratoire de Génétique des Procaryotes – Bruxelles – L. Van Malderen

ULg – Centre de Biophysique Moléculaire Numérique – Gembloux – L. Lins & R. Brasseur

ULg – CiTOS – Center for Integrated Technology and Organic Synthesis – Liège – J.C. Monbaliu


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ULg – Centre de Recherches du Cyclotron – Chimie Organique de Synthèse – Liège – A. Luxen &

G. Garraux ULg – Chimie Biologique Industrielle – AgroBioTech Gembloux – A. Richel

ULg – CSL – Centre Spatial de Liège – Liège – P. Gailly

ULg – Département de Biologie, Ecologie et Evolution – Morphologie ultrastructurale – Liège – P. Compère

ULg – Département de Chimie – Liège – C. Damblon

ULg – Département de Chimie – Laboratoire de Spectométrie de Masse – Liège – E. De Pauw

ULg - Département de Chimie – Nano-chimie et Systèmes Moléculaires – Liège –A.S. Duwez

ULg – Département de Chimie – Chimie des Macromolécules et des Matériaux Organiques – Liège - C. Jérôme ULg – Département de Chimie – Laboratoire de génie chimique – Liège – N. Job

ULg – Département de Géologie – Paléobotanique, Paléopalynologie, Micropaléontologie – Liège – E. Javaux ULg – Département des Sciences Biomédicales et Précliniques/Bactériologie, mycologie, parasitologie, virologie – Liège – P. Melin

ULg – Département des Sciences Biomédicales et Précliniques/Embryologie – Centre d’Immunologie – Liège – V. Geenen

ULg – Département des Sciences Cliniques – Liège – A. Gothot

ULg – Département des Sciences Cliniques / Pneumologie-Allergologie – Liège – R. Louis

ULg – Département des Sciences et Gestion de l’Environnement – Liège – M. Poulicek

ULg - Département des Sciences de la Vie – InBioS – Phylogénomique des eucaryotes – Liège – D. Baurain

ULg - Département des Sciences de la Vie – InBioS – Ecologie végétale et microbienne – Liège – M. Carnol ULg - Département des Sciences de la Vie – Biologie et génétique moléculaire – Liège – M. Figueroa

& C. Van de Weerdt ULg – Département des Sciences de la Vie – Photobiologie – Liège – F. Franck

ULg - Département des Sciences de la Vie – InBioS – Génomique fonctionnelle et imagerie moléculaire végétale – Liège – M. Hanikenne

ULg - Département des Sciences de la Vie – Génétique des algues – Liège – C. Remacle

ULg - Département des Sciences de la Vie – InBioS – PhytoSYSTEMS – Liège – P. Tocquin


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ULg - Gembloux Agro-Bio Tech – Microbial processes and interactions (MiPI) – Gembloux– P.

Jacques, F. Delvigne, P. Fickers & M. Ongena

ULg – GIGA Neurosciences – Liège – L. Bettendorf

ULg – GIGA-R – Physiologie Cellulaire et Moléculaire – Liège – F. Bureau

ULg – GIGA-R – Département des Sciences clinique – Liège – J. Caers

ULg – GIGA-Neuroscience – Liège – P. Leprince

ULg – GIGA Neurosciences – Biologie cellulaire et tissulaire – Liège – M. Thiry

ULg - University Hospital of Liège – Department of Clinical Microbiology - M.P. Hayette VUB –MINT Microbial Interactions – Rhode-Ste-Genèse – P. Cornelis

VUB – Plant Science and Nature Management – Brussels – L. Triest

X-Press Biologics – Milmort – M. Daukandt, A. Di Paolo & P. Ledent

BRAZIL

University of Sao Paulo – M. Fiore Botanical Garden of Sao Paulo – C. Sant’Anna

BULGARIA Stefan Angeloff Institute of Microbiology – Sofia – M. Angelova

CANADA Université Laval – Département de Biologie – Québec – W. Vincent

CHILE Universidad de Concepcion, Facultad de Ciencas ambientales EULA – Concepcion – R. Urrutia

CZECH REPUBLIC

Academy of Sciences of the Czech Republic – Institute of Botany – Trebon – J. Elster

University of South Bohemia – Faculty of Biological Sciences – Ceske Budejovice – J. Komarek

FRANCE AFFILOGIC – Nantes – M. Cinier Aix Marseille Université – Laboratoire de Chimie bactérienne – Marseille – M. Foglino

CEA – Institut de Recherche Technologique et des Sciences du Vivant, Laboratoire de Chimie et Biologie des Métaux – V. Forge & C. Marquette

CEA Saclay - Laboratoire Léon Brillouin – Gif-sur-Yvette – S. Longeville


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CNRS - Populations, Génétique et Evolution - Gif-sur-Yvette – J.L. Da Lage Ecole Centrale Marseille – AMU iSm2 – Marseille – J. Leclaire

Laboratoire des amino acides, peptides et protéines - Faculté de Pharmacie, Montpellier - Montpellier - J.-F. Hernandez Laboratoire de Bio-cristallographie - Institut de Biologie et Chimie des Protéines – Lyon - N. Aghajari & R. Haser Institut Pasteur – Unité de Biologie et Génétique de la Paroi bactérienne – Paris – I. Gomperts-

Boneca Institut Pasteur – Génétique des Génomes bactériens – Paris et Amabiotics - Evry - A. Danchin Institut Pasteur – Collections de cyanobactéries – Paris – M. Gugger

Montpellier SupAgro – Montpellier – M. Nigen

Nano-H S.A.S. – Lyon – C. Louis

Université d’Artois – Laboratoire de la Barrière Hémato-encéphalique – Lens – M. Culot

Université de Bretagne Occidentale – Brest – M. Le Romancer

Université de Caen - Laboratoire de Chimie Moléculaire et Thio-organique - Ensicaen - Caen - M.

Gulea Université Claude Bernard Lyon 1 – Laboratoire de Physico-Chimie des Matériaux Luminescents – Lyon – O. Tillement & F. Lux

Université Denis Diderot, Paris VII – Laboratoire ITODYS – Paris - F. Maurel

Université Joseph Fourier – Institut de Biologie Structurale – Laboratoire de Cristallographie Macromoléculaire - Grenoble – A. Dessen

Université Joseph Fourier – Institut de Biologie Structurale – Laboratoire de Cristallographie et Cristallogenèse des Protéines – Grenoble – J.L. Ferrer

Université Joseph Fourier – Institut de Biologie Structurale – Laboratoire de Résonance Magnétique Nucléaire – Grenoble – J.P. Simorre

Université Joseph Fourier – Institut de Biologie Structurale – Laboratoire d’Ingénierie des Macromolécules – Grenoble – T. Vernet

Université de Nantes – GEPEA UMR CNRS 6144 – Saint-Nazaire – L. Marchal

Université Paris VI – Laboratoire de Recherche Moléculaire sur les Antibiotiques – M. Arthur

Université Paris Sud – Laboratoire de Chimie Physique – Paris – M. Desouter

Université Paris Sud – Laboratoire Ecologie, Systématique et Evolution– Orsay – J. Kroymann


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Université Paris Sud – Laboratoire des enveloppes bactériennes – Orsay – D. Mengin Lecreulx & D.

Blanot

Université René Descartes – Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques – Y. le Merrer

Université de Technologie de Compiègne – Compiègne – S. Padiolleau

GERMANY Institute of Marine Biotechnology – Greifswald- T. Schweder RWTH-Aachen - Bioanalytics - Institut für Molekulare Biotechnologie - Aachen - K. Hoffmann University of Bayreuth – Laboratory of Biochemistry and Bayreuth Centre for Molecular Biological Sciences - Bayreuth - F. X. Schmid

University of Bochum- Departement for Biology and Biotechnology– Bochum – U. Krämer

University of Kaiserslautern – Department of Microbiology – Kaiserslautern – R. Hakenbeck

Martin Luther University – Halle-Wittenberg – J. Balbach

University of Wuppertal – Faculty of Mathematics and Natural Sciences – Department of Food Chemistry – M. Petz & D. Buty

GREECE University of Crete- Department of Biology – Heraklion - V. Bouriotis IRELAND Trinity College – Dublin – M. Caffrey

ITALY International School for Advanced Studies – Trieste – P. Calligari University of L’Aquila – Department of Sciences and Biochemical Technologies – M.G. Perilli & G.

Amicosante University of Modena and Reggio Emilia – Department of Chemistry – Modena – F. Prati

University of Naples Federico II - Department of Organic Chemistry and Biochemistry - G. Marino

& L. Tutino University of Padua - CRIBI Biotechnology Centre - Padua - P. Polverino de Laureto

University of Rome Tor Vergata – Department of Biology – Roma – D. Bili

University of Siena – Department of Molecular Biology - Siena - J.D. Docquier

University of Udine – Department of Biomedical and Biological Sciences– Udine – A. Corrazza &

G. Esposito


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LUXEMBURG Centre de Recherche Public de la Santé – Laboratoire de Rétrovirologie – Strassen – A. Chevigné

Centre de Recherche Public Gabriel Lipmann – Luxemburg – P. Delfosse & M. Calusinska Centre de Recherche Public de la Santé – Laboratoire d’Immunogénétique et d’Allergologie – Strassen – F. Hentges, C. Hilger & A. Kuehn

POLAND Gdansk University – Department of Biotechnology – Gdansk – M. Waleron

Medical University of Gdansk – Department of Pharmaceutical Microbiology – Gdansk – K. Waleron

SLOVENIA Jozef Stefan Institute - Department of Biochemistry and Molecular Biology - Ljubljana - R. H. Pain

University of Ljubljana – Department of Pharmaceutical Chemistry – Ljubljana – S. Gobec

SPAIN Autonomous University of Madrid – Biology Department – Madrid – A. Quesada

Cajal Institute – Consejo Superior de Investigaciones Científicas – Madrid – R. Moratalla

INIBIC – Microbiology – University College Hospital A Coruña – G. Bou

University of Granada – Química Física – F. Conejero-Lara

SWITZERLAND Basilea Pharmaceutica International Ltd – Basel – M.G.P. Page

Université de Genève – Faculté des Sciences Pharmaceutiques – Genève – E. Alleman

THAILAND

Chulalongkorn University – Division of Allergy and Clinical Immunology - Bangkok – A. Jacquet

THE NETHERLANDS Leiden University - Leiden Institute of Biology - Leiden - G. van Wezel

Utrecht University – Biochemistry of Membranes – Bijvoet Center – Utrecht – E. Breukink

UNITED KINGDOM British Antarctic Survey – Cambridge – D. Hodgson, P. Convey & D. Pearce

The James Hutton Institute - Dundee – J. Brown

Sekisui Diagnostics UK – West Malling – Kent – E. Asilonu


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University of Cambridge - Structural Chemistry and Spectroscopy - Department of Chemistry - Cambridge – A. Buell & C. M. Dobson

University of Leicester – Department of Molecular and Cell Biology – Leicester – G.C.K. Roberts

University of Leeds - Division of Microbiology, School of Biochemistry and Molecular Biology - Faculty of Biological Sciences - Leeds - I. Chopra University College of London – Department of Chemistry – F. Meersman

University of Newcastle - The Centre for Bacterial Cell Biology – Newcastle – W. Vollmer

University of Oxford - Department of Biochemistry - Oxford - C. Redfield

University of Oxford – Department of Chemistry – Oxford – L.J. Smith

University of Oxford – Oxford Centre for Molecular Sciences – Oxford – C. Schofield

University of Stirling – Department of Biology - Dundee – G. Codd

USA California State University Bakersfield - Department of Biology - I. Francis Desert Research Institute – Division of Earth and Ecosystem Sciences – Reno – A. Murray

Harvard Medical School – Microbiology and Immunobiology – Boston – R. Kolter Ohio State University – Plant Cellular and Molecular Biology – Columbus – P. Hamel

The Scripps Research Institute, Scripps Florida, Lead Identification, Translational Research Institute - Jupiter (Floride) - P. Hodder University of Akron – Department of Biology – Akron – H. Barton

University of California – Chemistry and Biochemistry - Los Angeles – S. Merchant

University of California, Berkeley – Plant and Microbial Biology - M. Traxler University of Florida – Center of Heterocyclic Chemistry – Gainesville – A. Katritzky

University of Florida – Department of Plant Pathology – Gainesville – R. Loria

University of Florida – IFAS – Fort Lauderdale Research and Education Center – Davie – H.D

Laughinghouse

University of Missouri-Kansas City – Division of Pharmaceutical Sciences – Kansas City – W. G.

Gutheil Vanderbilt University – Computational Chemical and Structural Biology – Nashville – J. Meiler

Wesleyan University – Department of Chemistry – Middletown – R.F. Pratt


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STAYS IN OTHER INSTITUTIONS Meriem El Ghachi, Trinity College Dublin, Ireland, March 29 – April 1, 2016

Olatunji Samir, Trinity College Dublin, Ireland, April 11-22, 2016

Annick Wilmotte, Universidad de Concepcion, Facultad de Ciencias ambientales EULA, Chile,

January 8-19, 2017


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VISITORS Adamou Arouna Omar, Hôpital Aristide Le Dantec, Dakar, Sénégal, November 16, 2015 – February 11, 2016 Almanza Maroquin Viviana, University of Concepcion, Chile, October 3 – November 28, 2017 Conceção Natalia, Instituto Federal de Educação, Ciência e Tecnologia de Rondônia (IFRO-Colorado do Oeste), Brazil, November 30 – December 23, 2016 Ghiglione Barbara, University of Buenos Aires, Argentina, May 2 – May 31, 2017 Ourri Benjamin, University Claude Bernard, Lyo, France, March 13 – March 17, 2017 Piccirilli Alessandra, University of L’Aquila, Italy, March 1 – May 31, 2017 Puschkareva Ekaterina, University of Ceske Budejovice, Czech Republic, March 7 – April 4, 2016

FUNDING

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Belspo PAI-IAP

FUNDING

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Politique Scientifique Fédérale Belge PAI P7/44 (2012-2017) - Integrative Protein Science: from small molecules to complex biological systems (the CIP is the Coordinator) BELSPO SD/BA/01A (2012-2017) - CCAMBIO: Antarctic Microbial Diversity and Climate Change BELSPO BRAIN-BE network project: Saving Freshwater Biodiversity Research Data (SAFRED), 2015-2018 BELSPO BRAIN-BE network project BR/165/A1: Diversity and function of microbiomes in the region of the Sør Rondane Mountains, Eastern Antarctica (MICROBIAN), 2016-2021 PRESPHOTO BR/132/A6 (2013-2016) - Preservation of photosynthetic microalgae of BCCM collections (www.presphoto.ulg.ac.be) BCCM/ULC Culture Collection of (sub)polar cyanobacteria (http://bccm.belspo.be/about-us/bccm-ulc) SPF Santé Publique (2017-2020) – RU-BLA-ESBL-CPE ? RF 17/6317: Emergence or decline of classical beta-lactamases (BLAC), of cephalosporinases (BLAAmpC), of extended spectrum beta-lactamases (BLAESBL), and of carbapenemases (BLACPE) amongst coliform enterobacteria from bovines: encoding gene identification and antibody neutralization

Les Actions de Recherche Concertées ARC-SF 12/16-04 (2012-2016) – NetRBI: Modelling of the Network Regulating Bacillus licheniformis BlaP -Lactamase Induction

Fonds de la Recherche Scientifique - FNRS

Mandats de recherche Mandat FNRS de Chercheur Temporaire Postdoctoral : - Dr Samir Olatunji (15/06/13 au 06/06/16) convention FRFC 2.4543.12 - Dr Marylène Vandevenne (01/10/14 au 30/09/17) CRCH -1.B409.15

Fonds de la Recherche Fondamentale Collective FRFC - T.0206.13 – PDR (2013-2017) – Analysis of metal hyperaccumulation and hypertolerance in Arabidopsis halleri: from population to protein FRFC - T.0006.14 - PDR (2014 - 2018) - Patscab: Etude des mécanismes d'induction de la formation de la gale commune de la pomme de terre par l'agent pathogène Streptomyces scabies

FUNDING

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Région Wallonne Convention 6956 – LEGOMEDIC (2012-2018) relative à un partenariat d’innovation technologique mis en œuvre par le pôle de compétitivité MECATECH Convention WBHealth 1318056 - MONALISA (2014 -2017) - MONitoring of Antibiotic Levels: from laboratory to IntenSive cAre units Convention 1318159 – Financement Equipement – Infrastructure de Recherche (lié au programme EQUIP 2013) – Projet ROBOTEINE ( 2014-2016) – Développement d’une plateforme de clonage, d’expression, de purification et d’analyse reposant sur des methods originals à haut debit développées et validées au laboratoire. Convention WB Health 1318058 - MYCAVERT (2014-2016) - Développement d’un produit pour la prévention des dermatophytoses au moyen d’inhibiteurs spécifiques des protéases fongiques Convention WB Health 1318044 - HOMECELLS (2014-2017) - Une structure nanofibrillaire tridimensionnelle pour l’ingénierie tissulaire et la médecine régénérative Convention 7273 - SINGLE CELLS (2015- 2017) relative à un partenariat d’innovation technologique mis en œuvre par le pôle de compétitivité Wagralim Convention REWARD 1410283 – Programme BEWARE Fellowships Academia (2015-2017) Convention 7225 - CARMAPHARM (2015-2017) - CARbon based MAtrix for PHARMaceutical purpose Convention 7550 – First Entreprise (2016-2018) – Optimization of Bacillus coagulans sporulation PICASSO Convention 1510472 – First Haute Ecole – SARDetect (2016-2018) – Mise au point de la detection de bactéries SARM par morphogranulométrie optique (partenaire du projet porté par la Haute Ecole HELMO) Convention 1510530 – First Spin Off – AntiPred (2016-2017) – Prédiction in silico des conditions de production de nouvelles biomolecules d’intérêt medical et agro-industriel par les microorganisms Convention 1510631 – BEWARE ACADEMIA – PRO4STAB (2016-2018) Convention 16100518 - BEWARE ACADEMIA – AUTOBMP-2 (2017-2018) Convention 16103741 – BEWARE ACADEMIA – P4XPRESS (2017-2018)

Bilateral Cooperation Wallonie/Bruxelles WBI International-Pologne (2014-2016) - Approche de génomique fonctionnelle pour caractériser l'expression des gènes empêchant les transferts génétiques et les réponses aux stress environnementaux des souches d'Arthrospira (ARTHRO-ARN) WBI International-Pologne (2017-2019) – Athrobiome, diversity, function and biotechnological application of the Arthrospira microbiome

FUNDING

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Union Européenne COST Action ES1105 – CYANOCOST (2012-2016) – Cyanobacteria blooms and toxins in water

resources: occurrence, impacts and management

COST Action TD1308 (2013-2018) - Origins and evolution of life on Earth and in the Universe

(ORIGINS)

CEE-Contract HEALTH-F3-2013-602906 (2014-2018) - Therapeutic Beta-Lactams MONitoring for STRATified and dose- adjusted treatment of hospital-acquired pneumonia: improved efficacy, decreased treatment length, and reduction of emergence of resistance (Mon4Strat) Convention ERA-Net 1510352 – EuroNanoMed II JTC 2015 (2016-2019) – DiaSyn: Development of a new in vivo radiotracer for aSynuclein Mandat post-doc BelPD Cofund Marie Curie : Dr Fabien Borderie (01/11/2015 au 30/07/2016)

Université de Liège

Crédits classiques Projet FSRC-12/115 (2013-2016) – Dr M. Dumoulin Analyses d’échantillons microvolumiques Projet FSRC-14/90 (2014-2018) – Dr S. Rigali AntiKarst : évaluation des potentialités d'actinomycètes karstiques à produire des métabolites d'intérêt thérapeutique

MISSIONS OF EXPERTISE

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Member of Research Councils

Moreno Galleni o Membre du Conseil sectoriel de la Recherche « Sciences et Techniques » (2009 - ) o Membre du Conseil universitaire de la Recherche (2009 - )

Member of Editorial Boards

Georges Feller – Extremophiles (2004 - ) Moreno Galleni – Antimicrobial Agents and Chemotherapy (2001 - ) Jean-Marie Frère – Antimicrobial Agents and Chemotherapy (2001 - ) Annick Wilmotte – Plant Ecology and Evolution (2010 - ) Mireille Dumoulin – International Journal of Rare Diseases & Orphan Drugs (2016 - )

Member of the Editorial Advisory Panels

Georges Feller – Biologia (Bratislava) (2002 - )

Member of the Evaluation Committees

Mireille Dumoulin

o Appel à projets Pasteur INNOV2016 o Al Jalila Foundation Research Center o Habilitation à Diriger des Recherches (HDR), Université de Cergy Pontoise, France o INNOVIRIS – Brussels o I-SITE ULNE project, Université Lille Nord – Europe Bernard Joris o Evaluation Committee for « Laboratoire de Procédés Biologiques, Génie Enzymatique et

Microbien (ProBioGEM) », Université de Lille 1, France (Scientific expert) o Evaluation committee for "Prospective Research for Brussels" (Jury member) o Evaluation of proposals ANR (France), Microbiology, Immunity and Infection « Panel of experts »

o The Joint Programming Initiative on Antimicrobial Resistance JPI-AMR, European Commission “Peer reviewer panel”

André Matagne Member of the evaluation Committee for the Picardie Région, « Santé, vivant » (2012 - 2017) Mohammed Terrak Project evaluation for the Czech Science Foundation Annick Wilmotte o Evaluation Committee for a VUB senior academic position in Microbiology, Free University of

Brussels (2015-2016) o 39th Antarctic Treaty Consultative Meeting – 19th Committee on Environmental Protection Meeting

– Santiago de Chile – Scientific expert of the Belgian delegation (2016)

MISSIONS OF EXPERTISE

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o 40th Antarctic Treaty Consultative Meeting – 20th Committee on Environmental Protection Meeting Beijing, China – Scientific expert of the Belgian delegation (2017)

o Priority Threat Management for Antarctic Biodiversity Workshop - Expert to identify the management strategies available to mitigate threats to Antarctic biodiversity and quantify the cost, feasibility and benefit of each action – Leuven , Belgium, July 8-9, 2017

o EU-PolarNet White Paper Workshop – Five white papers touching upon the most pressing issues in the Polar Regions” as a lead author for the redaction of the White Paper on Polar Biology/ La Cristaleria, Spain, September 23-28, 2017

International fora

Annick Wilmotte Scientific advisor of the Belgium Delegation to the Committee for Environmental Protection (CEP) of the Antarctic Treaty (since 2008)

COMMITTEES & SOCIETIES

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Charlier Paulette o Comité National Belge de Cristallographie (représentant ULg) (Vice-president) o Groupe de contact F.R.S.-FNRS « Rayonnement Synchrotron » (Secretary) Duez Colette o Groupe de contact F.R.S.-FNRS « Belgium Interdisciplinary Biofilm Research » (Secretary) Dumoulin Mireille o Belgian Biophysical Society (Member) o National Committee for Biophysics (Member) Frère Jean-Marie o Académie Royale de Belgique, Classe des Sciences (Vice-Directeur)

Galleni Moreno o BioLiège (Member) Joris Bernard o BioLiège (President) Kerff Frédéric o Belgian Biophysical Society (Member) o Scientific Reports (Editor) Matagne André o American Society for Biochemistry and Molecular Biology (Member) o Belgian Biophysical Society (Board member) o Belgian Society for Biochemistry and Molecular Biology (Board member) o Executive Council of the European Biophysical Societies’Association (EBSA) (Member) o F.R.S.-FNRS Contact group on Structural Biology (President) o Graduate doctoral school (F.R.S.-FNRS) on Structure and Function of Biological Macromolecules,

Bioinformatics and Modelling (SFMBBM) (President) o National Committee of Biochemistry and Molecular Biology (Board member) o National Committee of Biophysics (Member) o The Association of Resources for Biophysical Research in Europe (ARBRE) and Management

Committee of the Molecular Biophysics in Europe (MOBIEU) (Member) COST action (CA15126 – Between Atom and Cell: Integration Molecular Biophysics Approaches for Biology and Healthcare, for the period 2016 – 2020). Active participation in WG4 (Optimisation of data quality and scientific output consolidation)

o Elected titular member of the Royal Academy of Sciences in Belgium since February 27, 2016

Rigali Sébastien o Belgian Society for Microbiology (Member) o FRS-FNRS Contact group Molecular Bacteriology

Wilmotte Annick o American Society for Microbiology (ASM) (Member) o Phycological Society of America (PSA) (Member) o Belgian National Committee on Antarctic Research of the Academies of Sciences (Vice-Secretary) o Belgian National Committee for Microbiology, Royal Academy of Belgium (Member) o Belgian Society for Microbiology (Member) o Royal Belgian Botanical Society (Member) o COST Action ES1105 – Cyanobacteria blooms and toxins in water resources: Occurrence, impacts

and management (CYANOCOST) 2012-2016 (Belgian Delegate)

COMMITTEES & SOCIETIES

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o TD COST Action TD1308 – Origins and evolution of life on earth and in the universe (ORIGINS)

2014-2018 (Belgian Alternate Delegate) o Scientific Advisory Board of the project ECOPOLARIS, Czech Republic (Member) o Special Committee on the Harmonization of Nomenclature of Cyanophyta/Cyanobacteria

(Member) o Steering group of the ANT-ECO programme of the Scientific Committee on Antarctic Research

(http://www.scar.org./anteco/anteco-members) (Member) o SCAR Life Sciences Group (Belgian delegate) o Subcommittee for the Taxonomy of Phototrophic Bacteria of the International Committee on

Systematic Bacteriology (ICSB) (Secretary)

COMPOSITION OF THE CENTER

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Managing Committee

Director Paulette Charlier Executive Committee Paulette Charlier, Georges Feller, Moreno Galleni, Bernard Joris, André Matagne Managing Committee Alain Brans, Paulette Charlier, Colette Duez, Mireille Dumoulin, Georges Feller, Moreno Galleni, Colette Goffin, Bernard Joris, Frédéric Kerff, André Matagne, Sébastien Rigali, Mohammed Terrak, Annick Wilmotte Scientific Advisors Jacques Coyette, Martine Distèche, Jean-Marie Frère

Administrative Staff

Fabrice Raymond (Executive secretary) Fabienne Julémont (Administrative secretary)

Technical Assistance

Kim Beets, Caroline Bortuzzo, Nicole Gérardin-Otthiers, Raphaël Herman, Alexandre Lambion, Anne-Marie Matton, Joël Moray, Marine Renard, Charly Robert, Patricia Simon, Iris Thamm

Temporary Members

Researchers

Dr Ana Amoroso Dr Kishore Babu Bobbili Dr Fabien Borderie Dr Ahlem Bouaziz Mr Fabrice Bouillenne Ms Charlotte Crahay Dr Michaël Delmarcelle M. Mathieu Dondelinger Dr Meriem El Ghachi

Ms Astrid Freichels Dr Mareike Jakobs Dr Ruth Kellner Dr Yannick Lara Mr François Legrand Dr Serge Leimanis Ms Linda Menzer Dr Paola Mercuri Dr Caroline Montagner

Dr Aymeric Naomé Dr Samir Olatunji Dr Eric Sauvage Mr Patrick Stefanic Dr Elodie Tenconi Dr Julie Vandenameele Dr Marylène Vandevenne Mr Olivier Verlaine Dr Anna Wypijewska del Nogal

COMPOSITION OF THE CENTER

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PhD Students

Delphine Adam Francesco Amisano Sinaeda Anderssen Adrien Boes Madeleine Boulanger Frédéric Cawez Oscar Crasson Ismahene Dahmane Marjorie Dauvin Thomas Dauvrin Benoît Deflandre Simona De Franco

François Delbrassine Benoît Durieu Youssef El Fattahi Régine Freichels Samuel Jourdan Jeanne-Françoise Kabanyana Jennifer Kay Sophie Leclercq Gilles Lekeux Raphaël Léonard Marta Maciejewska Maxime Maréchal

Cristina Elisa Martina Loïc Martinet Alice Raymackers Charly Robert Frédéric Roulling Valentina Savaglia Igor Stelmach Pessi Edwige Van der Heyden Alessia Vercio Loïc Wetzels

2016-2017 report - labos ulglabos.ulg.ac.be/.../sites/19/2016/06/ra2016-2017-1.pdf · academy of...

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