1 / 26

IMMUNOGLOBULIN STRUCTURE AND FUNCTION

IMMUNOGLOBULIN STRUCTURE AND FUNCTION. September 20, 2006. THE TWO FORMS OF ANTIBODY. Membrane form is on the surface of B cells. Plasma cells make the secreted form which is found plasma, lymph, and interstitial fluid. The secreted form can also be found on the surface of cells with FcR.

nickan
Télécharger la présentation

IMMUNOGLOBULIN STRUCTURE AND FUNCTION

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  1. IMMUNOGLOBULIN STRUCTURE AND FUNCTION September 20, 2006

  2. THE TWO FORMS OF ANTIBODY Membrane form is on the surface of B cells Plasma cells make the secreted form which is found plasma, lymph, and interstitial fluid. The secreted form can also be found on the surface of cells with FcR

  3. IMMUNOGLOBULINS HAVE 4 POLYPEPTIDE CHAINS 2 Identical H(eavy) chains 2 Identical L(ight) chains

  4. HEAVY AND LIGHT CHAINS HAVE VARIABLE AND CONSTANT REGIONS

  5. ANTIBODY MOLECULES HAVE GLOBULAR REGIONS The globular regions are separated by a hinge region The globular regions contain globular domains

  6. THE STRUCTURE OF THE DOMAINS PROVIDES STABILITY Domains are approximately 110 amino acids Amino acids are aligned in b sheets V and C are slightly different

  7. ANTIBODY MOLECULES CAN BE CLEAVED BY PROTEOLYTIC ENZYMES Cleavage separates functionally distinct parts of protein

  8. Figure 3-4 HINGE REGION PROVIDES FLEXIBILITY Electron micrographs of ag-ab interaction demonstrates flexibility

  9. WU AND KABAT PLOTS REVEAL REGIONS OF HYPERVARIABILITY

  10. HYPERVARIABLE REGIONS ARE LOCATED IN DISCRETE LOOPS

  11. AN ANTIBODY BINDS AN EPITOPE OF THE ANTIGEN Antibody molecule binds epitopes on a viral particle

  12. Figure 3-8 Antigen Binding Site Can Have Different Shapes 4 types: pocket, groove, extended surface and protruding surface

  13. THE DIFFERENT CLASSES OF ANTIBODY There are two types of L chain: k and l There are 5 types of H chain: g, m, d, a, e A complete antibody molecule has 2 identical light chains and 2 identical heavy chains

  14. EACH ISOTYPE HAS SPECIFIC PROPERTIES AND FUNCTIONS

  15. IgM AND IgA CAN FORM MULTIMERS

  16. ANTIGENIC PROPERTIES OF IMMUNOGLOBULINS

  17. Isotypes have selective distribution

  18. POLYMERIC ISOTYPES CAN BE TRANSCYTOSED

  19. BACTERIA CAUSE DISEASE BY SECRETING TOXINS

  20. High Affinity IgG and IgA Can Neutralize Toxins

  21. High Affinity IgG and IgA Can Inhibit Viral Infection

  22. Ig Can Block Adherence of Bacteria IgA at mucosal surfaces IgG at other sites

  23. OPSONIZATION (IgG and IgA) Opsonization requires matching between FcR and Ig

  24. ADCC(IgG) ADCC also requires FcR and Ig isotype matching

  25. MAST CELL DEGRANULATION (IgE)

  26. FUNCTION AND DISTRIBUTION OF Ig ISOTYPES

More Related