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A lack of confirmed HPAIV epitopes recognized by cytotoxic T lymphocytes (CTLs) has hindered the utilization of CD8<sup>+</sup> T-cell-mediated immunity and has precluded the development of effectively diversified epitope-based vaccination approaches. In particular, an HPAIV H5N1 CTL-recognized epitope based on the peptide MHC-I-\u03b22m (pMHC-I) complex has not yet been designed. Here, screening a collection of selected peptides of several HPAIV strains against a specific pathogen-free pMHC-I (pBF2*1501), we identified a highly-conserved HPAIV H5N1 CTL epitope, named HPAIV-PA<sub>123-130</sub> We determined the structure of the BF2*1501-PA<sub>123-130</sub> complex at 2.1 \u00c5 resolution to elucidate the molecular mechanisms of a preferential presentation of the highly-conserved PA<sub>123-130</sub> epitope in the chicken B15 lineage. Conformational characteristics of the PA<sub>123-130</sub> epitope with a protruding Tyr-7 residue indicated that this epitope has great potential to be recognized by specific TCRs. Moreover, significantly increased numbers of CD8<sup>+</sup> T cells specific for the HPAIV-PA<sub>123-130</sub> epitope in peptide-immunized chickens indicated that a repertoire of CD8<sup>+</sup> T cells can specifically respond to this epitope. We anticipate that the identification and structural characterization of the PA<sub>123-130</sub> epitope reported here could enable further studies of CTL immunity against HPAIV H5N1. Such studies may aid in the development of vaccine development strategies using well-conserved internal viral antigens in chickens.","bibjson":{"author":[{"initials":"X","lastname":"Li","name":"Li X"},{"initials":"L","lastname":"Zhang","name":"Zhang L"},{"initials":"Y","lastname":"Liu","name":"Liu Y"},{"initials":"L","lastname":"Ma","name":"Ma L"},{"initials":"N","lastname":"Zhang","name":"Zhang N"},{"initials":"C","lastname":"Xia","name":"Xia C"}],"identifier":[{"id":"10.1074/jbc.RA120.012713","type":"doi"},{"id":"32152225","type":"pubmed"}],"issue":["16"],"journal":{"iso_abbreviation":"J Biol Chem","name":""},"pages":["5292-5306"],"title":"Structures of the MHC-I molecule BF2*1501 disclose the preferred presentation of an H5N1 virus-derived epitope.","type":"article","url":"https://www.sciencedirect.com/science/article/abs/pii/S0021925817485504","volume":["295"],"year":[2020]},"in_pmc":"N","in_pmce":"Y","open_access":"N"},"resolution":"2.90","same_as":{"pdbe":{"url":"https://www.ebi.ac.uk/pdbe/entry/pdb/6kx9"},"rcsb":{"url":"https://www.rcsb.org/structure/6kx9"}},"species":{"common_name":"Chicken","match_type":"histo:assign_species","scientific_name":"Gallus gallus","slug":"gallus_gallus"},"tcr":null,"title":"Gaga-BF2*015:01 binding \"RRALREGY\" at 2.90&#8491; resolution","unique_chain_count":3}}