Patent Report

This section provides Information on worldwide patents relevant to vaccine design and production. The Patent Report gives the following mformat~on: t~tle of patent, patentee, patent number, pubhcation date and summary of the patent. A number of patents m this report are reproduced from 'Blotechnology Abstracts' with permission of Derwent Publications Lid, Rochdale House, 128 Theobalds Road, London WC1X 8RD Telephone 071 242 5823; Fax 071 405 3630

Vaccine for combating Bordetella pertussis; new vaccine comprising 92 kDa, 38 kDa outer membrane protein, outer membrane vesicle, and pertussis toxin Ned. Mm. Health Pubhc Health and Cult World 9205 194, 2 April 1992

A vaccine (I) statable for combating Bordetella pertussls, comprismg as active component at least one or more outer membrane proteins (OMPs) derived from B pertussts, is new Also claimed are: 1. a method for the vaccination of humans, in particular children less than 2 years old, m which an effective amount of (I) is used; and li OMPs and outer membrane vesicles (OMVs) derived from B. pertussls, suitable for use in the preparation of (I) More specifically, B. pertussts is chosen from strain 134, 509, Tohama or BP-TOX6. The OMVs are derived from B. pertussls BP509, tim-mutant or the B pertussls BP 509 FHA-mutant. The OMPs have a mol wt of about 92 000, 32 000 and 38 000, the 92 000 OMP/38 000 weight ratio being especmlly more than 0.4. Additional components m the vaccine may be the pertussis toxin tOxold and/or FHA, optionally in the form of a divalent conjugate The vaccine provides effective protection against B pertussts m humans and is non-toxic and acellular and so there are none of the deleterious side effects associated with the whole-cell vaccine

089-92

Vaccine against Actinobacillus pleuropneumoniae; fermentation and purification Nippon Zenyaku Jpn 4077 437, 11 March 1992

A new vaccine against Actmobacillus pleuropneumomae (APP) ~s produced by growth of APP in stat~c culture or with gentle agitation, cell d~sintegration using glass beads, centrifuging the crushed cells to obtain a cell-free extract, removing contaminating substances from the extract by column chromatography, or opuonally by ultrafiltration, orgamc solvent extraction, affinity chromatography using a monoclonal anubody or lsoelectrlc prec~pltatlon The vaccine is preferably applied with phosphate-buffered saline at a concentration of 0.05-5 mg protem/ml, and may be administered l.m as a single or double administration. The vaccine is composed of lipid, sacchandes and proteins, and induces cellular lmmumty as well as antibody-producing activity. The compound prevents APP mfecuon at a low concentration in mice, guinea-pigs, p~gs, etc In an example, APP type-5 K17 was cultured in YCM culture medium (5 1) at 37°C for 6h The vaccine (380mg) was recovered by centrifugatlon, Dyno-mfll crushing and anion- exchange chromatography on a DE52 resin. 090-92

0264~410X/92/120886-02 ,~, 1992 Butterworth-Hememann Ltd

886 Vaccine, Vol 10, Issue 12, 1992

New mutant herpes simplex virus for use in vaccine e.g. HIV virus recombinant vaccine in attenuated vector Immunology World 9205 263; 2 April 1992

A new mutant v~rus has a genome defectwe in a gene essentml for production of Infectious virus, and ~s capable of protecting an Immunized susceptible species against infection by the corresponding wild-type virus. The mutant virus preferably contains an exogenous lmmunogentc protein gene in ItS genome. The mutant virus may be capable of estabhshing a latent refection with periodic reactivation in an infected species, e g herpes simplex v~rus with a defective glycoproteln gH gene The exogenous protein may be an lmmunodeficiency virus (e.g HIV virus) glycoproteln, and the recombinant virus may be used In a recombinant vaccine The new method combines the efficacy and safety of a killed vaccine w~th the extra immunological response reduced by m wvo production of viral protein by the attenuated vaccme The mutant virus may also be used as a safe vector for vaccination with a foreign protein, and It is possible to perform multiple effective vaccinations with the same virus vector Dosage can be relatively large, and ~t ~s unlikely that early events will be blocked by the host ~mmune response. 091 92

HIV virus gpl20 alloepitope peptide and related molecules; useful as passive and active vaccine against AIDS, for immunotherapy and in vivo imaging and in screening of new anti-AIDS drugs Hwer World 9205 196; 2 April 1992

The following are claimed' i a substance (I) which either recogntses an alloepitope of HIV virus gpl60 or its products, or recognlses C D 4 + T-cell receptors recognlsmg this aUoepltope or products, the alloepltope being associated with HIV virus gpl60 or its products when presented on, or m assoclauon with, a cell membrane, and which, in a CD4+ T-cell prohferatlon assay, stimulates proliferation of at least one CD4+ T cell clone; n (I) as above and having charged groups which adopts such a conformation when exposed to membrane-expressed gpl60, that the charged groups permit recogmtlon of gpl60 by the compound, the charged particles being complementary to the characteristic charged group of the major alpha-hehx of gpl20 in the region of amino acids 496-508; nL (I), preferably peptlde TRAKRRVVEREKR, exhibiting at least one portion of an alpha-hehcal secondary structure; iv. a vaccine against HIV-mduced AIDS comprising the substance of ( i ) and a carrier; v a passive vaccine against HIV-induced AIDS; w. use of the substances to raise antibodies, Wl. a diagnostic technique for the detection of the substances in ( l ) , VlU a diagnostic k~t 092-92

Hepatitis B virus vaccine containing new surface antigen; obtained by expression of recombinant surface antigen in Pichia pastoris which gives higher immunogenicity Cent Ing Genet. B1otechnol Eur 480 525, 15 April 1992

A new method for recovering hepautlS B virus surface antigen (HBVSAg) from Pwhta pastorls cells involves (1) lysls of the cells in a buffer, (2) precipitating contaminants at acidic pH; (3) subjecting the anugen preparation to adsorption on dmtomaceous earth and lmmunoaffinlty chromatography using a monoclonal antibody (mAb) specific for HBVSAg; and (4)