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Related Experiment Videos

Molecular components of T-cell recognition.

J L Jorgensen1, P A Reay, E W Ehrich

  • 1Department of Microbiology and Immunology, Stanford University, California 94305.

Annual Review of Immunology
|January 1, 1992
PubMed
Summary

The T cell receptor (TCR) interacts with antigenic peptides and MHC molecules. New data reveal TCR sensitivity to peptide conformation and flexible TCR-MHC contacts, impacting T-cell activation.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • The T cell receptor (TCR) recognizes peptide fragments presented by Major Histocompatibility Complex (MHC) molecules.
  • Understanding the ternary complex of TCR, peptide, and MHC is crucial for deciphering immune responses.

Purpose of the Study:

  • To review recent data enhancing the understanding of the TCR-peptide-MHC ternary complex.
  • To define the biochemical characteristics of peptide-MHC and TCR contact residues.
  • To elucidate the molecular basis of T-cell activation.

Main Methods:

  • Studies using synthetic peptide analogs and complete replacement sets.
  • Variant peptide immunization of TCR single-chain transgenic mice.
  • In vitro mutagenesis of MHC molecules and competition binding assays.

Main Results:

  • Peptide residues interacting with MHC and/or TCR were identified.
  • TCR exhibits high sensitivity to subtle peptide conformational changes.
  • Residues from V(D)J junctions of both TCR chains directly contact peptides.
  • TCR-MHC contacts are flexible and vary between TCRs.
  • TCR-peptide/MHC affinity is low (KD of 5 x 10(-5) M).

Conclusions:

  • T-cell activation likely initiates with antigen-independent adhesion.
  • The TCR binding site for peptides involves V(D)J junction residues.
  • TCR-MHC interactions are dynamic and adaptable.

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