ArticleProceedings of the National Academy of Sciences of the United States of America2021
Structurally silent peptide anchor modifications allosterically modulate T cell recognition in a receptor-dependent manner.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 36 citations in OpenAlex.
- HLA micropolymorphisms confine neoantigen conformational adaptability and guide T cell receptor selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dynamic Allostery in T Cell Receptor Specificity: A Role for Peptides and MHC Polymorphisms in Allosterically Tuning Immune Recognition.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Dynamical network analysis reveals long-range residue couplings at the pMHC interface underlying enhanced immunogenicity.NPJ systems biology and applications · 2026Article
- NeoPrecis: enhancing immunotherapy response prediction through integration of qualified immunogenicity and clonality-aware neoantigen landscapes.Nature communications · 2026Article
- β-amino acid substitution in the SIINFEKL antigen alters immunological recognition.Cancer biology & therapy · 2025Article
- Molecular Insights into Tumor Immunogenicity.Current issues in molecular biology · 2025Article
- NeoPrecis: Enhancing Immunotherapy Response Prediction through Integration of Qualified Immunogenicity and Clonality-Aware Neoantigen Landscapes.bioRxiv : the preprint server for biology · 2025Article
- A free energy perturbation-assisted machine learning strategy for mimotope screening in neoantigen-based vaccine design.Briefings in bioinformatics · 2025Article
- Integrative Computational Immunology Applied to Identify and Characterize CD8+ T-cell Neoepitopes of Shared KRAS Neoantigen Oncogenic Driver Hotspot Mutations.Asian Pacific journal of cancer prevention : APJCP · 2025Article
- nuTCRacker: Predicting the Recognition of HLA-I-Peptide Complexes by αβTCRs for Unseen Peptides.European journal of immunology · 2025Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Nature communications · 2025Article
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- Multi-Epitopic Peptide Vaccine Against Newcastle Disease Virus: Molecular Dynamics Simulation and Experimental Validation.Vaccines · 2024Article
- HLA A*24:02-restricted T cell receptors cross-recognize bacterial and preproinsulin peptides in type 1 diabetes.The Journal of clinical investigation · 2024Article
- Insights into therapeutic peptides in the cancer-immunity cycle: Update and challenges.Acta pharmaceutica Sinica. B · 2024Review
- SARS-CoV-2 spike does not interact with the T cell receptor or directly activate T cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Research square · 2024Article
- Tumor-Derived Antigenic Peptides as Potential Cancer Vaccines.International journal of molecular sciences · 2024Review
- APE-Gen2.0: Expanding Rapid Class I Peptide-Major Histocompatibility Complex Modeling to Post-Translational Modifications and Noncanonical Peptide Geometries.Journal of chemical information and modeling · 2024Article
- Structural basis for self-discrimination by neoantigen-specific TCRs.Nature communications · 2024Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Presentation of peptides by class I MHC proteins underlies T cell immune responses to pathogens and cancer. The association between peptide binding affinity and immunogenicity has led to the engineering of modified peptides with improved MHC binding, with the hope that these peptides would be useful for eliciting cross-reactive immune responses directed toward their weak binding, unmodified counterparts. Increasing evidence, however, indicates that T cell receptors (TCRs) can perceive such anchor-modified peptides differently than wild-type (WT) peptides, although the scope of discrimination is unclear. We show here that even modifications at primary anchors that have no discernible structural impact can lead to substantially stronger or weaker T cell recognition depending on the TCR. Surprisingly, the effect of peptide anchor modification can be sensed by a TCR at regions distant from the site of modification, indicating a through-protein mechanism in which the anchor residue serves as an allosteric modulator for TCR binding. Our findings emphasize caution in the use and interpretation of results from anchor-modified peptides and have implications for how anchor modifications are accounted for in other circumstances, such as predicting the immunogenicity of tumor neoantigens. Our data also highlight an important need to better understand the highly tunable dynamic nature of class I MHC proteins and the impact this has on various forms of immune recognition.
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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.