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MLRS 242 Immunology Pat Reed Antibodies Serum proteins General antibody structure Enzyme digestion fragments 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 Ribbon model of antibody Detailed structure of antibody Ribbon model of variable region • Variable region contains highly variable connecting regions called complementaritydetermining regions or CDRs • These regions are also shown to be the antigen binding sites Model of antibody Amino acid diversity of variable domains – complementaritydetermining regions (CDRs) Antigen – antibody interaction Space filling model Hiv protease and Fab fragment Conformational change in Fab domain General structures of different antibody classes Subclasses of IgG Secretory IgA Receptor bound IgE • Isotype – different species • Allotype – same species, different alleles • Idiotype – same species, different VH and VL domains Isotypic determinants – different species variation within the constant region Allotypic determinants – different constant regions within the same species – different alleles Idiotypic determinants – variations in the variable region within the same antibody type B Cell Receptor - BCR Fc receptors – bind Fc portion of antibody molecules Immunoglobulin superfamily of cell receptors – evolved from common ancestor gene More members of the Ig superfamily Monoclonal antibodies Many uses for monoclonal antibodies Antibodies can deliver drugs to specific targets