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...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Daichao Wu, D. Travis Gallagher, Ragul Gowthaman, Brian G. Pierce, Roy A. Mariuzza
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/539421cdbf2649ba84e049f00249ee1a
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:539421cdbf2649ba84e049f00249ee1a
record_format	dspace
spelling	oai:doaj.org-article:539421cdbf2649ba84e049f00249ee1a2021-12-02T17:34:47ZStructural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen10.1038/s41467-020-16755-y2041-1723https://doaj.org/article/539421cdbf2649ba84e049f00249ee1a2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16755-yhttps://doaj.org/toc/2041-1723Developing 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.Daichao WuD. Travis GallagherRagul GowthamanBrian G. PierceRoy A. MariuzzaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
title	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_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_sort	structural basis for oligoclonal t cell recognition of a shared p53 cancer neoantigen
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/539421cdbf2649ba84e049f00249ee1a
work_keys_str_mv	AT daichaowu structuralbasisforoligoclonaltcellrecognitionofasharedp53cancerneoantigen AT dtravisgallagher structuralbasisforoligoclonaltcellrecognitionofasharedp53cancerneoantigen AT ragulgowthaman structuralbasisforoligoclonaltcellrecognitionofasharedp53cancerneoantigen AT briangpierce structuralbasisforoligoclonaltcellrecognitionofasharedp53cancerneoantigen AT royamariuzza structuralbasisforoligoclonaltcellrecognitionofasharedp53cancerneoantigen
_version_	1718379939178217472

Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen

Ejemplares similares