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Hepatitis E Virus (HEV)-Specific T Cell Receptor Cross-Recognition: Implications for Immunotherapy.

Chai Fen Soon1,2, Shihong Zhang1, Pothakamuri Venkata Suneetha1

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Summary

Candidate T cell receptors (TCRs) for immunotherapy targeting hepatitis E virus (HEV) showed cross-reactivity to self-peptides. While dual-specific, the TCR was functional only against the viral target, highlighting the need for autoimmune screening in TCR development.

Keywords:
CD8+ T cellsT cell receptor (TCR)T cell therapyTCR redirectioncross-reactivityhepatitis E virus (HEV)immunotherapy

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Area of Science:

  • Immunology
  • Oncology
  • Virology

Background:

  • T cell immunotherapy utilizes cytotoxic T lymphocytes targeting tumor- or pathogen-specific antigens for cancer and infectious disease treatment.
  • Antigen-specificity of T cell receptors (TCRs) is crucial for immunotherapy design, but off-target reactivity to self-peptides raises autoimmunity concerns.
  • Hepatitis E virus (HEV)-specific TCRs were identified as potential candidates for treating chronic hepatitis E.

Purpose of the Study:

  • To investigate the potential cross-reactivity of an HEV-specific TCR (HEV-1527) with self-peptides, aiming to understand potential autoimmunity.
  • To explore the role of a unique multiple glycine motif in the TCR-β CDR3 region in mediating cross-reactivity.

Main Methods:

  • Identified HEV-specific TCRs targeting a HLA-A2-restricted epitope (HEV-1527: LLWNTVWNM).
  • Assessed cross-recognition of self-peptides using double Dextramer binding assays.
  • Evaluated functional responses of the TCR against both viral and self-antigens.

Main Results:

  • The HEV-1527 specific TCR demonstrated cross-recognition of an apoptosis-related self-peptide epitope from Nonmuscle Myosin Heavy Chain 9 (MYH9-478: QLFNHTMFI).
  • Despite dual specificity confirmed by Dextramer binding, the TCR was selectively functional against the HEV-1527 epitope and not the self-antigen.
  • A consecutive glycine motif in the TCR-β chain was suggested as a factor promoting binding promiscuity and cross-recognition.

Conclusions:

  • Candidate TCRs for immunotherapy should be rigorously screened for autoimmune potential, particularly those with unique sequence patterns like the glycine motif.
  • Selective functionality despite cross-recognition suggests a complex interplay between TCR structure, antigen binding, and immune response activation.