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How a single T cell receptor recognizes both self and foreign MHC.

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Summary

T cell receptors (TCRs) can recognize foreign and self-proteins, a process called alloreactivity. This study reveals that the 2C TCR uses distinct structural strategies to bind different major histocompatibility complex (MHC) ligands, challenging the idea of molecular mimicry in TCR crossreactivity.

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Alphabeta T cell receptors (TCRs) exhibit crossreactivity with self- and foreign- major histocompatibility complex (MHC) proteins, a phenomenon known as alloreactivity.
  • Understanding the structural basis of TCR recognition of diverse ligands is crucial for immunology and transplantation.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying the crossreactivity of the 2C TCR with different MHC-peptide complexes.
  • To compare how the 2C TCR engages a foreign ligand (H-2L(d)-QL9) versus a self-ligand (H-2K(b)-dEV8).

Main Methods:

  • X-ray crystallography was used to determine the 2.35 A structure of the 2C TCR complexed with H-2L(d)-QL9.
  • Comparative structural analysis of the 2C TCR bound to both foreign (H-2L(d)-QL9) and self (H-2K(b)-dEV8) ligands.

Main Results:

  • The 2C TCR employs divergent structural strategies to bind the foreign H-2L(d)-QL9 and self H-2K(b)-dEV8 ligands.
  • The TCR engages unique pairwise contacts with both MHC polymorphic residues and peptide antigens for each ligand.
  • Greater structural complementarity was observed between the 2C TCR and the L(d)-QL9 complex.
  • An engineered high-affinity TCR variant maintained the wild-type binding orientation despite altered TCR-CDR3alpha-peptide interactions.

Conclusions:

  • A single TCR can recognize distinct ligands through different binding mechanisms, indicating crossreactivity without molecular mimicry.
  • These findings provide novel insights into the structural basis of T cell receptor alloreactivity and ligand discrimination.