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

J Immunol. 1991 Mar 15;146(6):2017-20.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / physiology
  • Animals
  • Antibodies, Monoclonal / genetics*
  • Base Sequence
  • Immunoglobulin Variable Region / chemistry
  • Immunoglobulin Variable Region / genetics*
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Mutation
  • Phosphorylcholine / immunology*
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Antibodies, Monoclonal
  • Immunoglobulin Variable Region
  • Phosphorylcholine

Associated data

  • GENBANK/D10148
  • GENBANK/D10149
  • GENBANK/M58659
  • GENBANK/M58674
  • GENBANK/M58675
  • GENBANK/M60429
  • GENBANK/M60430
  • GENBANK/M60432
  • GENBANK/M60434
  • GENBANK/M60435