A V region mutation in a phosphocholine-binding monoclonal antibody results in loss of antigen binding

B. J. Kobrin, S. Buhl, M. J. Shulman, M. D. Scharff

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

A V region mutant producing an antibody that had lost the ability to bind phosphocholine was isolated from a hybridoma producing a germline encoded T15 antibody. The mutation resulted in a single aspartic acid to asparagine substitution at residue 95 of the H chain V region. This confirms that the aspartic acid at residue 95 plays a major role in Ag binding. The results also suggest that somatic cell genetic techniques can be used to generate mAb with useful changes in Ag binding.

Original languageEnglish (US)
Pages (from-to)2017-2020
Number of pages4
JournalJournal of Immunology
Volume146
Issue number6
StatePublished - Jan 1 1991

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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