IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts

Nature. 1981 May 7;291(5810):29-34. doi: 10.1038/291029a0.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibody Diversity*
  • Binding Sites, Antibody* / genetics
  • Choline / analogs & derivatives*
  • Clone Cells / immunology
  • Genes
  • Hybrid Cells / immunology
  • Immunoglobulin G* / genetics
  • Immunoglobulin Idiotypes / genetics
  • Immunoglobulin M* / genetics
  • Immunoglobulin Variable Region* / genetics
  • Mice
  • Mutation
  • Myeloma Proteins / genetics
  • Phosphorylcholine / immunology*

Substances

  • Immunoglobulin G
  • Immunoglobulin Idiotypes
  • Immunoglobulin M
  • Immunoglobulin Variable Region
  • Myeloma Proteins
  • Phosphorylcholine
  • Choline