ArticleThe Journal of clinical investigation2024
HLA A*24:02-restricted T cell receptors cross-recognize bacterial and preproinsulin peptides in type 1 diabetes.
Article in The Journal of clinical investigation, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Interplay Between Infectious Diseases and the Endocrine System: An Overview and Clinical Insights.Endocrinology, diabetes & metabolism · 2026Review
- Triple islet autoantibody-positive type 1 diabetes in Japanese stiff-person syndrome despite a protective HLA haplotype.JCEM case reports · 2026Article
- Is the NOD mouse a good model for type 1 diabetes?Diabetologia · 2026Review
- Frontier research and clinical application prospects of microbiome biomarkers in autoimmune diseases.Frontiers in immunology · 2026Review
- Augmented MHC Class I on Professional Antigen-Presenting Cells and Enhanced Cytokine Production by CD8European journal of immunology · 2025Article
- Fingerprint Profile Analysis ofPharmaceuticals (Basel, Switzerland) · 2025Article
- Immunopeptidomics for autoimmunity: unlocking the chamber of immune secrets.NPJ systems biology and applications · 2025Review
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- Microbial mimics supersize the pathogenic self-response.The Journal of clinical investigation · 2024Article
Corrections and comments
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Authors and funding
27 authors.
Funding
Abstract
CD8+ T cells destroy insulin-producing pancreatic β cells in type 1 diabetes through HLA class I-restricted presentation of self-antigens. Combinatorial peptide library screening was used to produce a preferred peptide recognition landscape for a patient-derived T cell receptor (TCR) that recognized the preproinsulin-derived (PPI-derived) peptide sequence LWMRLLPLL in the context of disease risk allele HLA A*24:02. Data were used to generate a strong superagonist peptide, enabling production of an autoimmune HLA A*24:02-peptide-TCR structure by crystal seeding. TCR binding to the PPI epitope was strongly focused on peptide residues Arg4 and Leu5, with more flexibility at other positions, allowing the TCR to strongly engage many peptides derived from pathogenic bacteria. We confirmed an epitope from Klebsiella that was recognized by PPI-reactive T cells from 3 of 3 HLA A*24:02+ patients. Remarkably, the same epitope selected T cells from 7 of 8 HLA A*24+ healthy donors that cross-reacted with PPI, leading to recognition and killing of HLA A*24:02+ cells expressing PPI. These data provide a mechanism by which molecular mimicry between pathogen and self-antigens could have resulted in the breaking of self-tolerance to initiate disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.