Meeuwsen, Miranda H., Wouters, Anne K., Hagedoorn, Renate S., Kester, Michel G. D., Remst, Dennis F. G., van der Steen, Dirk M., de Ru, Arnoud, van Veelen, Peter A., Rossjohn, Jamie ![]() |
Abstract
Unconventional HLA class I–restricted CD8+ T cell epitopes, longer than 10 aa, have been implicated to play a role in human immunity against viruses and cancer. T cell recognition of long peptides, centrally bulging from the HLA cleft, has been described previously. Alternatively, long peptides can contain a linear HLA-bound core peptide, with a N- or C-terminal peptide “tail” extending from the HLA peptide binding groove. The role of such a peptide “tail” in CD8+ T cell recognition remains unclear. In this study, we identified a 20mer peptide (FLPTPEELGLLGPPRPQVLA [FLP]) derived from the IL-27R subunit α gene restricted to HLA-A*02:01, for which we solved the crystal structure and demonstrated a long C-terminal “tail” extension. FLP-specific T cell clones demonstrated various recognition modes, some T cells recognized the FLP core peptide, while for other T cells the peptide tail was essential for recognition. These results demonstrate a crucial role for a C-terminal peptide tail in immunogenicity.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Medicine |
Publisher: | American Association of Immunologists |
ISSN: | 0022-1767 |
Date of Acceptance: | 16 February 2022 |
Last Modified: | 10 Nov 2022 11:23 |
URI: | https://orca.cardiff.ac.uk/id/eprint/150331 |
Citation Data
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