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Science 18 November 1983:
Vol. 222. no. 4625, pp. 721 - 726
DOI: 10.1126/science.6356353
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Articles

Science, Vol 222, Issue 4625, 721-726
Copyright © 1983 by American Association for the Advancement of Science

articles

Monoclonal antibodies reveal the structural basis of antibody diversity

JL Teillaud, C Desaymard, AM Giusti, B Haseltine, RR Pollock, DE Yelton, DJ Zack, and MD Scharff

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Tailor-Made Monoclonal Antibodies.
R. A. DePINHO, L. B. FELDMAN, and M. D. SCHARFF (1986)
Ann Intern Med 104, 225-233
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