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    Immunoglobulin Structure and Function

    , PhDMD

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    Immunogobulin, Ig

    What isImmunoglobulin?

    Immunoglobulins are the critical

    ingredients of humoral acquiredimmune response.

    The immunoglobulins are a group of

    glycoproteins present in the serum and

    tissue fluids of all mammals.

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    Immunoglobulins:Structure and

    Function Definition: Glycoprotein molecules that are

    produced by plasma cells in response to an

    immunogen and which function as antibodies

    Immune serum

    Ag adsorbed serum

    1 2

    + -

    albumin

    globulins

    Mobility

    Amount

    ofprotein

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    General Functions of

    Immunoglobulins

    Effector functions

    Fixation of complement

    Binding to mast cells , macrophages, NK cell

    (Usually require Ag binding)

    Ag binding

    Can result in protection

    Valence

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    Basic Immunoglobulin Structure

    Immunoglobulins - heterogeneous

    Myeloma proteins - homogeneous

    immunoglobulins

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    Two Forms ofImmunoglobulin

    Membrane-boundreceptor Soluble antibody

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    Immunoglobulin Structure

    Variable(V) &

    Constant (C)

    Regions

    VL & CL

    VH & CH

    Hinge Region

    CH1

    VL

    CL

    VH

    CH2

    CH3

    Hinge Region

    Carbohydrate

    Disulfide bond

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    Structural Regions

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    hypervariable

    region

    also called

    Complementarity

    Determining

    Regions(CDRs),

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    Immunoglobulin Fragments:

    Structure/Function Relationships

    Fab

    Ag binding

    Valence = 1

    Specificity

    determined by VH

    and VL

    Papain

    Fc

    Fab

    Fc ( crystallizable)

    Effector functions

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    DomainsofImmunoglobulin

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    Function ofImmunoglobulins

    Recognition of antigen

    Activation of complement

    Opsonization

    Antibody-dependent cell-mediated

    cytotoxicity,ADCC

    Mediate hypersensitivity type I

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    Immunoglobulin Classes and

    SubclassesImmunglobulin molecules are divided into

    distinct classes and subclasses in terms of

    the differences in amino acid sequence of

    constant region of heavy chain,

    i.e.,,,,andchains.

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    Immunoglobulin Classes ofMammals

    IgG - Gamma () heavy chains

    IgM - Mu () heavy chains

    IgA - Alpha () heavy chains IgD - Delta () heavy chains

    IgE - Epsilon () heavy chains

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    Five Classes ofImmunoglobulin

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    IgG has a family of subclass, IgG1, IgG2, IgG3,

    IgG4(cattle has no)

    IgA is divided into two subclasses, IgA1 and

    IgA2(sheep).

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    Light Chain Types ofImmunoglobulin

    Kappa ()

    Lambda ()

    All light chains have protein molecularweights of approximately 23,000 but can

    be divided into two distinct types, namely

    chain, chain, respectively

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    IgA

    Structure

    Serum - monomer

    Secretions (sIgA)

    Dimer (11S)

    J chain

    Secretory component

    JChainSecretory Piece

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    IgA

    Structure

    Properties

    2nd highest serumIg Major secretory Ig (Mucosal orLocal Immunity)

    Tears, saliva, gastric and pulmonary secretions

    Does not fix complement (unless aggregated)

    Binds to Fc receptors on some cells

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    IgD

    Structure

    Properties

    4th highest serumIg B cell surface Ig

    Does not bind complement

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    IgE

    Structure

    Properties

    Least common serumIg Binds to basophils and mast cells (Does not

    require Ag binding)

    Allergic reactions

    Parasitic infections (Helminths) Binds to Fc receptor on eosinophils

    Does not fix complement