Identification of a naturally processed HLA-A*02:01-restricted CTL epitope from the human tumor-associated antigen Nectin-4 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-10

AUTHORS

Marc Lopez, Abderrezak Ghidouche, Caroline Rochas, Danièle Godelaine, Javier Carrasco, Didier Colau, Gérald Hames, Félix A. Montero-Julian, Pierre G. Coulie, Daniel Olive

ABSTRACT

Nectin-4 is a tumor antigen present on the surface of breast, ovarian and lung carcinoma cells. It is rarely present in normal adult tissues and is therefore a candidate target for cancer immunotherapy. Here, we identified a Nectin-4 antigenic peptide that is naturally presented to T cells by HLA-A2 molecules. We first screened the 502 nonamer peptides of Nectin-4 (510 amino acids) for binding to and off-rate from eight different HLA class I molecules. We then combined biochemical, cellular and algorithmic assays to select 5 Nectin-4 peptides that bound to HLA-A*02:01 molecules. Cytolytic T lymphocytes were obtained from healthy donors, that specifically lyzed HLA-A2(+) cells pulsed with 2 out of the 5 peptides, indicating the presence of anti-Nectin-4 CD8(+) T lymphocytes in the human T cell repertoire. Finally, an HLA-A2-restricted cytolytic T cell clone derived from a breast cancer patient recognized peptide Nectin-4145-153 (VLVPPLPSL) and lyzed HLA-A2(+) Nectin-4(+) breast carcinoma cells. These results indicate that peptide Nectin-4145-153 is naturally processed for recognition by T cells on HLA-A2 molecules. It could be used to monitor antitumor T cell responses or to immunize breast cancer patients. More... »

PAGES

1177-1188

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00262-016-1877-7

DOI

http://dx.doi.org/10.1007/s00262-016-1877-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012906253

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27514672


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