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IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts

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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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Authors and Affiliations

  1. Department of Embryology, Carnegie Institution of Washington, 115 W. University Parkway, Baltimore, Maryland, 21210, USA

    Patricia J. Gearhart

  2. Division of Biology, California Institute of Technology, Pasadena, California, 91125, USA

    Nelson D. Johnson, Richard Douglas & Leroy Hood

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  1. Patricia J. Gearhart
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  2. Nelson D. Johnson
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  3. Richard Douglas
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  4. Leroy Hood
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Gearhart, P., Johnson, N., Douglas, R. et al. IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts. Nature 291, 29–34 (1981). https://doi.org/10.1038/291029a0

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