ArticleJCI insight2019
Mass spectrometry driven exploration reveals nuances of neoepitope-driven tumor rejection.
Article in JCI insight, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Comprehensive mapping of identical sequences across human proteins emphasizes the widespread issue of shared epitopes in self-antigens.NAR genomics and bioinformatics · 2026Article
- Structural changes from wild-type define tumor-rejecting neoantigens.Journal for immunotherapy of cancer · 2025Article
- Sensitive neoantigen discovery by real-time mutanome-guided immunopeptidomics.Nature communications · 2025Article
- A frameshift-generated cancer neoepitope that controls tumor burden in prophylaxis as well as therapy.Journal of immunology (Baltimore, Md. : 1950) · 2025Article
- Predicting MHC-I ligands across alleles and species: how far can we go?Genome medicine · 2025Article
- Low-avidity T cells drive endogenous tumor immunity in mice and humans.Nature immunology · 2025Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Nature communications · 2025Article
- NetMHCpan-4.2: improved prediction of CD8+ epitopes by use of transfer learning and structural features.Frontiers in immunology · 2025Article
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- Identification of immunogenic HLA class I and II neoantigens using surrogate immunopeptidomes.Science advances · 2024Article
- Crucial Parameters for Immunopeptidome Characterization: A Systematic Evaluation.International journal of molecular sciences · 2024Article
- Immunogenicity of Non-Mutated Ovarian Cancer-Specific Antigens.Current oncology (Toronto, Ont.) · 2024Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Research square · 2024Article
- NeoMUST: an accurate and efficient multi-task learning model for neoantigen presentation.Life science alliance · 2024Article
- Cancer neoepitopes viewed through negative selection and peripheral tolerance: a new path to cancer vaccines.The Journal of clinical investigation · 2024Review
- Neoantigen prioritization based on antigen processing and presentation.Frontiers in immunology · 2024Review
- Structural and physical features that distinguish tumor-controlling from inactive cancer neoepitopes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Immunopeptidome from a Genomic Perspective: Establishing the Noncanonical Landscape of MHC Class I-Associated Peptides.Cancer immunology research · 2023Article
- The MHC Motif Atlas: a database of MHC binding specificities and ligands.Nucleic acids research · 2023Article
- Recent advances in immunopeptidomic-based tumor neoantigen discovery.Advances in immunology · 2023Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Neoepitopes are the only truly tumor-specific antigens. Although potential neoepitopes can be readily identified using genomics, the neoepitopes that mediate tumor rejection constitute a small minority, and there is little consensus on how to identify them. Here, for the first time, we use a combination of genomics, unbiased discovery MS immunopeptidomics and targeted MS to directly identify neoepitopes that elicit actual tumor rejection in mice. We report that MS-identified neoepitopes are an astonishingly rich source of tumor rejection mediating neoepitopes. MS has also demonstrated unambiguously the presentation by MHC I, of confirmed tumor rejection neoepitopes which bind weakly to MHC I; this was done using DCs exogenously loaded with long peptides containing the weakly binding neoepitopes. Such weakly MHC I-binding neoepitopes are routinely excluded from analysis, and our demonstration of their presentation, and their activity in tumor rejection, reveals a broader universe of tumor-rejection neoepitopes than presently imagined. Modeling studies show that a mutation in the active neoepitope alters its conformation such that its T cell receptor-facing surface is significantly altered, increasing its exposed hydrophobicity. No such changes are observed in the inactive neoepitope. These results broaden our understanding of antigen presentation and help prioritize neoepitopes for personalized cancer immunotherapy.
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