ArticleNature communications2021
Reversion analysis reveals the in vivo immunogenicity of a poorly MHC I-binding cancer neoepitope.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Dynamic states of an MHC class I molecule during peptide exchange.Nature communications · 2026Article
- Lung cancer vaccines to enhance immune checkpoint inhibitor therapy: evidence and future perspectives.Journal of hematology & oncology · 2026Review
- Structural changes from wild-type define tumor-rejecting neoantigens.Journal for immunotherapy of cancer · 2025Article
- Immunologic specificity in glioblastoma: Antigen discovery and translational implications.Neuro-oncology advances · 2025Review
- A frameshift-generated cancer neoepitope that controls tumor burden in prophylaxis as well as therapy.Journal of immunology (Baltimore, Md. : 1950) · 2025Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Nature communications · 2025Article
- CryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Evolving T Cell Receptor Recognition Code: The Rules Are More Like Guidelines.Immunological reviews · 2025Review
- Review
- Metformin modulates mitochondrial autophagy in renal tubular epithelial injury induced by high glucose via the Keap1/Nrf2 pathway.Molecular and cellular biochemistry · 2024Article
- Dynamic allostery in the peptide/MHC complex enables TCR neoantigen selectivity.Research square · 2024Article
- Cancer neoepitopes viewed through negative selection and peripheral tolerance: a new path to cancer vaccines.The Journal of clinical investigation · 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
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Interferon-α promotes neo-antigen formation and preferential HLA-B-restricted antigen presentation in pancreatic β-cells.bioRxiv : the preprint server for biology · 2023Article
- Immunosurveillance shapes the emergence of neo-epitope landscapes of sarcomas, revealing prime targets for immunotherapy.JCI insight · 2023Article
- Article
- The 2022 Report on the Human Proteome from the HUPO Human Proteome Project.Journal of proteome research · 2023Review
- Human thymopoiesis produces polyspecific CD8eLife · 2023Article
- Germline-mediated immunoediting sculpts breast cancer subtypes and metastatic proclivity.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
16 authors at 5 institutions in 3 countries.
Funding
Abstract
High-affinity MHC I-peptide interactions are considered essential for immunogenicity. However, some neo-epitopes with low affinity for MHC I have been reported to elicit CD8 T cell dependent tumor rejection in immunization-challenge studies. Here we show in a mouse model that a neo-epitope that poorly binds to MHC I is able to enhance the immunogenicity of a tumor in the absence of immunization. Fibrosarcoma cells with a naturally occurring mutation are edited to their wild type counterpart; the mutation is then re-introduced in order to obtain a cell line that is genetically identical to the wild type except for the neo-epitope-encoding mutation. Upon transplantation into syngeneic mice, all three cell lines form tumors that are infiltrated with activated T cells. However, lymphocytes from the two tumors that harbor the mutation show significantly stronger transcriptional signatures of cytotoxicity and TCR engagement, and induce greater breadth of TCR reactivity than those of the wild type tumors. Structural modeling of the neo-epitope peptide/MHC I pairs suggests increased hydrophobicity of the neo-epitope surface, consistent with higher TCR reactivity. These results confirm the in vivo immunogenicity of low affinity or 'non-binding' epitopes that do not follow the canonical concept of MHC I-peptide 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.