IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts

PJ Gearhart, ND Johnson, R Douglas, L Hood - Nature, 1981 - nature.com
PJ Gearhart, ND Johnson, R Douglas, L Hood
Nature, 1981nature.com
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 …
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.
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