IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts

Patricia J. Gearhart, Nelson D. Johnson, Richard Douglas, Leroy Hood

Research output: Contribution to journalArticle

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 V H 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.

Original languageEnglish (US)
Pages (from-to)29-34
Number of pages6
JournalNature
Volume291
Issue number5810
DOIs
StatePublished - Dec 1 1981

    Fingerprint

ASJC Scopus subject areas

  • General

Cite this

Gearhart, P. J., Johnson, N. D., Douglas, R., & Hood, L. (1981). IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts. Nature, 291(5810), 29-34. https://doi.org/10.1038/291029a0