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. Scharf

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter describes how the analysis of closely related families of monoclonal antibodies has provided new insights into the structural basis of antigen binding and the molecular mechanism responsible for antibody diversity. While the ability to sample the repertoire of antibodies through the analysis of monoclonal antibodies can provide important insights, some questions are hard to answer with this approach. The chapter discusses the instability of immunoglobulin genes in cultured myeloma and hybridoma cells. The specificity of the interactions of monoclonal antibodies to the idiotype and monoclonal antibodies and myeloma proteins of known sequence illustrates both the benefits and complexities of trying to use reagents to identify chemical relatedness. Monoclonal antibodies that no longer react with one or a few of those anti-idiotypic monoclonals are presumptive variants. The large amount of paraprotein in the serum of patients or animals with the malignancy is a monoclonal antibody that is produced by a transformed antibody-forming cell growing in an uncontrolled fashion.

Original languageEnglish (US)
Title of host publicationBiotechnology and Biological Frontiers
PublisherTaylor and Francis
Pages291-302
Number of pages12
ISBN (Electronic)9780429705915
ISBN (Print)9780367020460
DOIs
StatePublished - Jan 1 2019
Externally publishedYes

ASJC Scopus subject areas

  • Social Sciences(all)

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    Teillaud, J. L., Desaymard, C., Giusti, A. M., Haseltine, B., Pollock, R. R., Yelton, D. E., Zack, D. J., & Scharf, M. D. (2019). Monoclonal antibodies reveal the structural basis of antibody diversity. In Biotechnology and Biological Frontiers (pp. 291-302). Taylor and Francis. https://doi.org/10.4324/9780429050329-24