Chapter 4. Antigen Recognition by B-cell and T-cell Receptors

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1 Chapter 4 Antigen Recognition by B-cell and T-cell Receptors

2 Antigen recognition by BCR and TCR B cells 2 separate functions of immunoglobulin (Ig) bind pathogen & induce immune responses recruit cells and molecules to destroy the pathogen Functions of Ab neutralization T opsonization complement activation B M

3 Antigen recognition by BCR and TCR T cells T-cell receptor (TCR) recognizes short peptide fragments of Ags Major histocompatibility complex (MHC) show great genetic variation in the population MHC restriction TCR recognizes features of both MHC + peptides

4 Structure of a typical antibody molecule secreted form of B-cell receptor Y-shaped molecules V-regions - binding to wide variety of antigens C-regions interaction with effector cells and molecules Five different classes of Igs - IgA, IgD, IgE, IgG, IgM

5 Figure 3-1 General structure of an antibody molecule

6 Structure of a typical antibody molecule IgG Abs consist of 4 polypeptide chains MW- 50 kda of 2 H chain + 25 kda of 2 light chain = 150kDa 2 types of light chain lambda( ) and kappa ( ) to ratio 20:1 (mice), 2:1 (human), 1:20 (cattle) 5 isotype (heavy chain calsses) IgM ( ) IgD ( ) IgG ( ) IgA ( ) IgE ( )

7 IgG Abs consist of 2 heavy chains & 2 light chains that are joined by disulfide bonds 25kDa Lambda ( ) Kappa ( ) 50kDa

8 Five main heavy-chain classes (isotype) IgA ( ), IgD ( ), IgE ( ),IgG ( ), IgM ( )

9 Structure of a typical antibody molecule Immunoglobulin heavy and light chains are composed of constant and variable regions Amino acid sequences of Ab show 2 important features 1) similar sequences with 110 a.a. long - domain L chain 2 Ig domains H chain 4 Ig domains 2) N-terminal a.a. sequences of 1 st domain of both L and H chains vary greatly between different Abs Variable domains V domains Constant domains - C domains

10 Antibody molecule can readily be cleaved into functionally distinct fragments Fab (Fragment antigen binding) Fc (Fragment crystallizable)

11 F(ab )2 valuable therapeutic agents single chain Fv (fragment variable) - immunotoxin

12 Structure of a typical antibody molecule Immunoglobulin molecule is flexible, especially at hinge region Haptens small molecule, which can be recognized by Ab but are able to stimulate production of anti-hapten Abs only when linked to a larger protein carrier

13 Antibody Fab s are joined by a flexible hinge region, thus allowing independent movement of the 2 antigen binding sites

14 Structure of a typical antibody molecule Domains of immunoglobulin molecule have similar structures barrel - 2 sheets Structure of V and C domains is essentially similar Main difference between V and C domains is that V is larger, with an extra loop Common a.a. of C and V domains is essential for its stability immunoglobulin superfamily

15 Domain structure of immunoglobulin constant & variable (V) regions

16 Interaction of antibody molecule with specific antigen Localized regions of hypervariable sequence form antigen-binding site Sequence variability of V region is concentrated in certain segments hypervariable regions

17 The V regions of immunoglobulin H & L chains consist of hypervariable & less variable (framework region) sequences Variability plot

18 The hypervariable regions lie in discrete loops that link the strands characteristic of the immunoglobulin fold

19 Interaction of antibody molecule with specific antigen Abs bind Ags via contacts with amino acids in CDRs, but details of binding depend upon size and shape of Ag

20 The antigen binding sites of different antibodies can differ in size and shape

21 Interaction of antibody molecule with Abs bind to conformational shapes on surface of Ags specific antigen Antigenic determinant or epitope structure recognized by Ab Conformational or discontinuous epitope epitope composed of protein segments that are discontinuous in aa seq.of Ag but are brought together in 3D structure Continuous or linear epitope epitope composed of a single protein segment Synthetic peptides in vaccines

22 Ag-Ab interactions involve a variety of forces Antibodies bind to their cognate antigens via various types of noncovalent forces

23 Model based on X-ray crystallography data of an anti-lysozyme Fab bound to hen egg white lysozyme (HEL) - H chain in dark blue - L chain in yellow - HEL in aquamarine blue A critical glutamine HEL residue that is part of the epitope bound by the antibody is in red.

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