Monoclonal antibodies reveal the structural basis of antibody diversity

Jean Luc Teillaud, Catherine Desaymard, Angela M. Giusti, Barbara Haseltine, Roberta R. Pollock, Dale E. Yelton, Donald J. Zack, Matthew D. Scharff

Research output: Contribution to journalArticlepeer-review

53 Scopus citations

Abstract

Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.

Original languageEnglish (US)
Pages (from-to)721-726
Number of pages6
JournalScience
Volume222
Issue number4625
DOIs
StatePublished - 1983

ASJC Scopus subject areas

  • General

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