IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts.
An amino acid sequence analysis of the N-terminal immunoglobulin heavy and light chain variable regions (VH and VL) from 16 hybridoma proteins which bind phosphorylcholine as well as the complete sequence analysis of 9 of these VH regions is presented. There seem to be more VH regions participating in the phosphorylcholine response than can be encoded directly by germ-line VH gene segments. Moreover, the V regions from IgG antibodies are considerably more variable than those from their IgM counterparts. These observations raise the possibility that a somatic mechanism for V region diversification produces greater diversity in IgG than in IgM antibodies.
D000595:Amino Acid Sequence; D000818:Animals; D000916:Antibody Diversity; D001666:Binding Sites, Antibody / Q000235:genetics; D002794:Choline / Q000031:analogs & derivatives*; D002999:Clone Cells / Q000276:immunology; D005796:Genes; D006822:Hybrid Cells / Q000276:immunology; D007074:Immunoglobulin G / Q000235:genetics; D007130:Immunoglobulin Idiotypes / Q000235:genetics; D007075:Immunoglobulin M / Q000235:genetics; D007135:Immunoglobulin Variable Region / Q000235:genetics; D051379:Mice; D009154:Mutation; D009194:Myeloma Proteins / Q000235:genetics; D010767:Phosphorylcholine / Q000276:immunology*
D007074:Immunoglobulin G; D007130:Immunoglobulin Idiotypes; D007075:Immunoglobulin M; D007135:Immunoglobulin Variable Region; D009194:Myeloma Proteins; D010767:Phosphorylcholine; D002794:Choline