Profound alteration in an αβ T-cell antigen receptor repertoire due to polymorphism in the first complementarity-determining region of the β chain

S. J. Gahm, B. J. Fowlkes, S. C. Jameson, N. R.J. Gascoigne, M. M. Cotterman, O. Kanagawa, R. H. Schwartz, L. A. Matis

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Amino acid residues that are critical in maintaining the framework structure of immunoglobulin heavy- and light-chain variable (V) regions are strongly conserved in the Vα and Vβ proteins of the αβ T-cell antigen receptor (TCRαβ). Consequently, it has been proposed that TCRαβ has a conformation similar to that of an immunoglobulin Fab fragment and that the regions of the TCR homologous to the three immunoglobulin complementarity- determining regions (CDRs 1, 2, and 3) bind to the peptide antigen-major histocompatibility complex (MHC) molecule ligand. A single amino acid substitution in the predicted CDR1 of the Vβ3 protein of certain mouse strains dramatically altered TCRαβ usage in an antigen-specific MHC- restricted immune response but did not abrogate Vβ3 specificity for the superantigens minor lymphocyte stimulatory locus (Mls)(c) and staphylococcal enterotoxin A (SEA). The results confirm the importance of the Vβ CDR1 in antigen-MHC molecule recognition, supporting the Fab-like structural model of TCRαβ, and provide further evidence that conventional antigen-MHC recognition and superantigen recognition are mediated by distinct regions of the TCR β chain. They also suggest that allelic polymorphism may be a significant source of diversity in the TCR repertoire.

Original languageEnglish (US)
Pages (from-to)10267-10271
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number22
DOIs
StatePublished - 1991

Keywords

  • T-cell antigen recognition
  • allelic polymorphism

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