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    Immunoglobulin: Ig, Ig, Ig

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    Rhea Ong
    Immunoglobulins, also known as antibodies, are Y-shaped proteins that have four polypeptide chains connected by disulfide bonds and a hinge region. They function to bind to antigens and carry out effector functions like complement fixation. The structure of immunoglobulins allows for their function and variation. The five major classes are IgM, IgE, IgD, IgG, and IgA, which differ in location, amount, function, and comments. IgM is the first to react to infection while IgE mediates allergic reactions. Little is known about IgD.

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    Immunoglobulin: Ig, Ig, Ig

    Uploaded by

    Rhea Ong
    99 views29 pages
    Immunoglobulins, also known as antibodies, are Y-shaped proteins that have four polypeptide chains connected by disulfide bonds and a hinge region. They function to bind to antigens and carry out effector functions like complement fixation. The structure of immunoglobulins allows for their function and variation. The five major classes are IgM, IgE, IgD, IgG, and IgA, which differ in location, amount, function, and comments. IgM is the first to react to infection while IgE mediates allergic reactions. Little is known about IgD.

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    Immunoglobulin

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    Immunoglobulins, also known as antibodies, are Y-shaped proteins that have four polypeptide chains connected by disulfide bonds and a hinge region. They function to bind to antigens and carry out effector functions like complement fixation. The structure of immunoglobulins allows for their function and variation. The five major classes are IgM, IgE, IgD, IgG, and IgA, which differ in location, amount, function, and comments. IgM is the first to react to infection while IgE mediates allergic reactions. Little is known about IgD.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    99 views29 pages

    Immunoglobulin: Ig, Ig, Ig

    Uploaded by

    Rhea Ong
    Immunoglobulins, also known as antibodies, are Y-shaped proteins that have four polypeptide chains connected by disulfide bonds and a hinge region. They function to bind to antigens and carry out effector functions like complement fixation. The structure of immunoglobulins allows for their function and variation. The five major classes are IgM, IgE, IgD, IgG, and IgA, which differ in location, amount, function, and comments. IgM is the first to react to infection while IgE mediates allergic reactions. Little is known about IgD.

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    of 29

    IMMUNOGLOBULIN

    IgM, IgE, IgD

    Rhea Ong, DMD

    objectives
    To discuss function To discuss structure to know classification of immunoglobulin

    terms
    Immunoglobulin Fab

    Immunoglobulin
    TWO Roles
    plasma membrane bound antigen receptors on the surface of a B-cell as antibodies free in cellular fluids

    *antibody function is intimately related to its structure

    GENERAL FUNCTIONS OF IMMUNOGLOBULINS


    A. Antigen binding B. Effector Functions 1.Fixation of complement 2.Binding to various cell types

    pointers
    AB
    - The valency of antibody refers to the number of antigenic determinants that an individual antibody molecule can bind
    EF - biological effects are a consequence of secondary "effector functions" of antibodies *binding of an antibody to an antigen has no direct biological effect *usually the ability to carry out a particular effector function requires that the antibody bind to its antigen

    pointers
    immunoglobulins mediate a effector functions Not every immunoglobulin will mediate all effector functions

    Basic Immunoglobulin Structure


    1. Four polypeptide chains: two "light" chains two "heavy" chains 2. Disulfide (-S-S-) bonds 3. Hinge Region

    LIGHT CHAIN
    220 amino acids

    Constant 110 amino acids


    variable 110 amino acids
    Hypervariable* Framework region Framework region

    HEAVY CHAIN
    440-550 amino acids

    Constant 110 amino acids variable 340-440 amino acids


    Hypervariable* Framework region

    pointers
    heavy chain an immunoglobulin determines the immunoglobulin "isotype - classification IgA IgG IgM IgE IgD

    constant variable
    Hypervariable Framework region

    pointers
    Hypervariable Epitope is found

    IMMUNOGLOBULIN FRAGMENTS: STRUCTURE/FUNCTION RELATIONSHIPS

    pointers
    Fab

    - The combining site of the antibody is created by both VH and VL


    Fc - contains the remainder of the two heavy chains each containing a CH2 and CH3 domain

    pointers
    Functions are either
    Independent of the particular class Dependent of the particular class

    GENERATION OF ANTIBODY DIVERSITY


    Multiple genes in the germ line DNA Variable recombination during differentiaion of the germ line cells into B-cells Mutations during differentiaion of the germ line cells into B-cells

    Multiple genes in the germ line DNA

    Variable recombination

    Mutations

    pointers
    The immune System has the capacity to recognize and respond to about 10,000,000

    Heavy Chain (VDJ)- 200 X 12 X 4 = 9600 Light Chain (VJ)- 200 X 5 = 1000

    9,600,000

    IMUNNOGLOBULIN PRODUCTION
    Rearrangement Recombination Mutation

    DIFFERENT TYPES OF IMMUNOGLOBULIN

    IgM IgE IgD

    IgM
    Heavy chain: Mu Its mean concentration in serum is 0.4-2.5 mg/mL with a half-life of 7 days first immunoglobulin to be generated by a neonate. It is also the EARLIEST immunoglobulin to be produced after exposure to a novel antigen Due to its pentameric structure, it has multiple antigen binding sites which results in overall high molecular valency- IgM plays an important role in the process of agglutination There are no subclasses of IgM

    IgE
    Heavy chain: EPSILON Its mean concentration in serum is less than 0.0005 mg/mL (NB IgE is the least abundant Ig in human serum) with half life of 2 days (NB IgE can have much longer half-life if surface-bound) Despite its low concentrations in serum, IgE has a very high potency. It binds Fc receptors on MAST CELL and BASOPHILS, and thereby triggers ALLERGIC reactions - by activation of mast cells and subsequent release of HISTAMINE and other inflammatory mediators (TNF-Alpha; prostaglandins; leukotriens; platelet activating factor; and cytokines IL-4 and IL-13 to perpetuate TH2 response) IgE has no recognised subclasses

    IgD
    Heavy chain: DELTA Its mean concentration in serum is less than 0.03 mg/mL with a half-life of 2 days Monomeric structure only IgD does not activate complement or cross the placenta It is highly unstable in serum and chiefly found on the surface of B cells rather than on its own Thus, its main function is to act as a RECEPTOR for CELL ACTIVATION IgD has no subclasses

    SUMMARY

    Function
    Antigen binding Effector function

    Parts of Immunoglobulin
    Disulfide bonds Hinge region

    Fxn related to structure


    Fc

    Variation
    Isotype dependent independent

    4 polypeptide chain Fab

    location IgM IgE Blood and lymph fluid Mucuous membrane, skin, Lungs Tissue that line the belly and chest

    Numbers 5-10% little

    Fuction AB AB

    Comment 1st to react largest Allergic reactions Parasitic reaction Maybe on B cell surface Little is known

    IgD

    Least abundant AB

    Discussions
    first immunoglobulin (Ig) to react to an infection is IgM if your IgM is high, then it is an acute infection. Then next to react is IgG, if it is high, then it is a chronic infection, 2 weeks or more. If both IgM and IgG arre in the normal range, then the infection must have been neutralized. IgE if its a parasitic infestation.

    IgE if its a parasitic infestation. Little is known of IgD

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