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T cell receptors (TCRs) can recognize diverse antigens through unexpected structural rearrangements, not just molecular mimicry. This finding challenges current models of T cell cross-reactivity and immune recognition.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Structural Biology

Background:

  • T cell receptors (TCRs) enable a limited repertoire to recognize a vast array of antigens.
  • Previous research highlighted peptide structural and chemical homology, rather than sequence, in TCR cross-reactivity.
  • However, TCRs can cross-react with ligands lacking significant physiochemical similarities.

Purpose of the Study:

  • To investigate the mechanisms underlying T cell receptor cross-reactivity between divergent antigens.
  • To explore how the T cell receptor DMF5 recognizes antigens with minimal commonalities.

Main Methods:

  • Studied the clinically relevant T cell receptor DMF5.
  • Analyzed antigen recognition mechanisms involving peptide and MHC protein rearrangements.
  • Investigated binding-induced peptide register shifts and extensions from MHC peptide binding grooves.

Main Results:

  • Demonstrated that T cell receptor cross-recognition of divergent antigens can occur via unanticipated peptide and MHC protein rearrangements.
  • Identified binding-induced peptide register shifts and extensions from MHC peptide binding grooves as key mechanisms.
  • Showed that cross-reactivity is possible even without structural or chemical molecular mimicry.

Conclusions:

  • Established novel principles governing T cell receptor cross-reactivity beyond molecular mimicry.
  • Highlighted the role of dynamic structural rearrangements in antigen recognition by T cells.
  • Implications for predicting and controlling T cell specificity and challenges in predicting T cell reactivities.