Replacements in the exposed loop of the T15 antibody VH CDR2 affect carrier recognition of PC-containing pathogens

McKay Brown, Gregory D. Wiens, Thomas O'Hare, Mary P. Stenzel-Poore, Marvin B. Rittenberg

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A panel of mutant antibodies of the phosphocholine (PC)-binding antibody, T15, was tested for binding to PC-protein, Streptococcus pneumoniae, Trichinella spiralis and Ascaris suum. Relative to wildtype T15, all the mutant antibodies showed differential recognition of the panel of PC- associated antigens. These mutant antibodies contain amino acid replacements in the CDR2 region of the heavy chain variable region, indicating the importance of CDR2 in recognition of carrier determinants. A model of T15 is shown that illustrates the strategic placement of mutations that could allow interaction with determinants associated with PC. A direct implication of this finding is that the T15 antibody combining site accommodates structures larger than phosphocholine and that recognition of associated carrier determinants could be a significant force in shaping the immune response to PC-containing pathogens.

Original languageEnglish (US)
Pages (from-to)205-211
Number of pages7
JournalMolecular Immunology
Volume36
Issue number3
DOIs
StatePublished - Feb 1 1999

Keywords

  • Antibody CDR
  • Mutation
  • Phosphocholine
  • T15 antibody

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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