Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen
Developing broadly applicable neoantigen-directed adoptive cell therapies (ACTs) is challenging because each cancer patient has an unique neoantigen repertoire. Here, the authors present the crystal structures of tumor-specific T cell receptors (TCRs) that recognize a shared neoepitope arising from...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2020-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-16755-y |
| _version_ | 1819037004927598592 |
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| author | Daichao Wu D. Travis Gallagher Ragul Gowthaman Brian G. Pierce Roy A. Mariuzza |
| author_facet | Daichao Wu D. Travis Gallagher Ragul Gowthaman Brian G. Pierce Roy A. Mariuzza |
| author_sort | Daichao Wu |
| collection | DOAJ |
| description | Developing broadly applicable neoantigen-directed adoptive cell therapies (ACTs) is challenging because each cancer patient has an unique neoantigen repertoire. Here, the authors present the crystal structures of tumor-specific T cell receptors (TCRs) that recognize a shared neoepitope arising from the R175H driver mutation in the p53 oncogene (p53R175H) alone and bound to p53R175H–HLA-A2, which are of interest for the structure-guided design of TCRs to improve T cell potency for ACT. |
| first_indexed | 2024-12-21T08:14:32Z |
| format | Article |
| id | doaj.art-539421cdbf2649ba84e049f00249ee1a |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-21T08:14:32Z |
| publishDate | 2020-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-539421cdbf2649ba84e049f00249ee1a2022-12-21T19:10:36ZengNature PortfolioNature Communications2041-17232020-06-0111111210.1038/s41467-020-16755-yStructural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigenDaichao Wu0D. Travis Gallagher1Ragul Gowthaman2Brian G. Pierce3Roy A. Mariuzza4W.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology ResearchW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology ResearchW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology ResearchW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology ResearchW.M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology ResearchDeveloping broadly applicable neoantigen-directed adoptive cell therapies (ACTs) is challenging because each cancer patient has an unique neoantigen repertoire. Here, the authors present the crystal structures of tumor-specific T cell receptors (TCRs) that recognize a shared neoepitope arising from the R175H driver mutation in the p53 oncogene (p53R175H) alone and bound to p53R175H–HLA-A2, which are of interest for the structure-guided design of TCRs to improve T cell potency for ACT.https://doi.org/10.1038/s41467-020-16755-y |
| spellingShingle | Daichao Wu D. Travis Gallagher Ragul Gowthaman Brian G. Pierce Roy A. Mariuzza Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen Nature Communications |
| title | Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen |
| title_full | Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen |
| title_fullStr | Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen |
| title_full_unstemmed | Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen |
| title_short | Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen |
| title_sort | structural basis for oligoclonal t cell recognition of a shared p53 cancer neoantigen |
| url | https://doi.org/10.1038/s41467-020-16755-y |
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