1. MLRS 242 Immunology Pat Reed Antibodies

2. Serum proteins

3. General antibody structure

4. Enzyme digestion fragments

5. Protein structure of immunoglobulins
Early amino acid sequence experiments were unsuccessful—too much variation
Multiple myeloma serum is 95% same antibody
Bence-jones protein found in urine of myeloma patients is excess light chain
110 amino acids highly variable, rest are quite constant
5 different isotypes identified: based on type of heavy chain: G,D,E,M,A
Human light chains: 60% kappa (K) chains, 40% lambda (L) chains

7. Ribbon model of antibody

8. Detailed structure of antibody

10. Ribbon model of variable region
Variable region contains highly variable connecting regions called complementarity-determining regions or CDRs
These regions are also shown to be the antigen binding sites

11. Model of antibody

13. Amino acid diversity of variable domains – complementarity- determining regions (CDRs)

14. Antigen – antibody interaction

15. Space filling model

16. Hiv protease and Fab fragment Conformational change in Fab domain

18. General structures of different antibody classes

24. Subclasses of IgG

26. Secretory IgA

27. Receptor bound IgE

28. Isotype – different species
Allotype – same species, different alleles
Idiotype – same species, different VH and VL domains

29. Isotypic determinants – different species variation within the constant region

30. Allotypic determinants – different constant regions within the same species – different alleles

31. Idiotypic determinants – variations in the variable region within the same antibody type

32. B Cell Receptor - BCR

33. Fc receptors – bind Fc portion of antibody molecules

34. Immunoglobulin superfamily of cell receptors – evolved from common ancestor gene

35. More members of the Ig superfamily

36. Monoclonal antibodies

37. Many uses for monoclonal antibodies

38. Antibodies can deliver drugs to specific targets