ArticleProceedings of the National Academy of Sciences of the United States of America2022
Physical and in silico immunopeptidomic profiling of a cancer antigen prostatic acid phosphatase reveals targets enabling TCR isolation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Overcoming T cell tolerance to tumor self-antigens through catch-bond engineering.Science (New York, N.Y.) · 2026Article
- Defining T cell receptor repertoires using nanovial-based binding and functional screening.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- IRIS: Discovery of cancer immunotherapy targets arising from pre-mRNA alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Defining T cell receptor repertoires using nanovial-based affinity and functional screening.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
25 authors at 4 institutions in 1 country.
Funding
Abstract
Tissue-specific antigens can serve as targets for adoptive T cell transfer-based cancer immunotherapy. Recognition of tumor by T cells is mediated by interaction between peptide-major histocompatibility complexes (pMHCs) and T cell receptors (TCRs). Revealing the identity of peptides bound to MHC is critical in discovering cognate TCRs and predicting potential toxicity. We performed multimodal immunopeptidomic analyses for human prostatic acid phosphatase (PAP), a well-recognized tissue antigen. Three physical methods, including mild acid elution, coimmunoprecipitation, and secreted MHC precipitation, were used to capture a thorough signature of PAP on HLA-A*02:01. Eleven PAP peptides that are potentially A*02:01-restricted were identified, including five predicted strong binders by NetMHCpan 4.0. Peripheral blood mononuclear cells (PBMCs) from more than 20 healthy donors were screened with the PAP peptides. Seven cognate TCRs were isolated which can recognize three distinct epitopes when expressed in PBMCs. One TCR shows reactivity toward cell lines expressing both full-length PAP and HLA-A*02:01. Our results show that a combined multimodal immunopeptidomic approach is productive in revealing target peptides and defining the cloned TCR sequences reactive with prostatic acid phosphatase epitopes.
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