{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T02:04:56Z","timestamp":1789610696073,"version":"build-2803163510"},"reference-count":63,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2016,8,1]],"date-time":"2016-08-01T00:00:00Z","timestamp":1470009600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"name":"The 863 Project of the China Ministry of Science and Technology","award":["2013AA102503"],"award-info":[{"award-number":["2013AA102503"]}]},{"DOI":"10.13039\/501100001809","name":"National Science Foundation of China","doi-asserted-by":"crossref","award":["31201887"],"award-info":[{"award-number":["31201887"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"The 973 Project of the China Ministry of Science and Technology","award":["2013C835302"],"award-info":[{"award-number":["2013C835302"]}]},{"DOI":"10.13039\/100012901","name":"The Youth Teacher Scientifc Research and Innovation Program of Zhoukou Normal University","doi-asserted-by":"crossref","award":["ZKNUB115208"],"award-info":[{"award-number":["ZKNUB115208"]}],"id":[{"id":"10.13039\/100012901","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2016,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The lack of a peptide-swine leukocyte antigen class I (pSLA I) complex structure presents difficulties for the study of swine cytotoxic T lymphocyte (CTL) immunity and molecule vaccine development to eliminate important swine viral diseases, such as influenza A virus (IAV). Here, after cloning and comparing 28 SLA I allelic genes from Chinese Heishan pigs, pSLA-3*hs0202 was crystalized and solved. SLA-3*hs0202 binding with s\u03b22m and a KMNTQFTAV (hemagglutinin [HA]-KMN9) peptide from the 2009 pandemic swine H1N1 strain clearly displayed two distinct conformations with HA-KMN9 peptides in the structures, which are believed to be beneficial to stimulate a broad spectrum of CTL immune responses. Notably, we found that different HA-KMN9 conformations are caused, not only by the flexibility of the side chains of residues in the peptide-binding groove (PBG), but also by the skewing of \u03b11 and \u03b12 helixes forming the PBG. In addition, alanine scanning and circular-dichroism (CD) spectra confirmed that the B, D, and F pockets play critical biochemical roles in determining the peptide-binding motif of SLA-3*hs0202. Based on biochemical parameters and comparisons to similar pockets in other known major histocompatibility complex class I (MHC-I) structures, the fundamental motif for SLA-3*hs0202 was determined to be X-(M\/A\/R)-(N\/Q\/R\/F)-X-X-X-X-X-(V\/I) by refolding\n            <jats:italic>in vitro<\/jats:italic>\n            and multiple mutant peptides. Finally, 28 SLA-3*hs0202-restricted epitope candidates were identified from important IAV strains, and two of them have been found in humans as HLA-A*0201-specific IAV epitopes. Structural and biochemical illumination of pSLA-3*hs0202 can benefit vaccine development to control IAV in swine.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            We crystalized and solved the first SLA-3 structure, SLA-3*hs0202, and found that it could present the same IAV peptide with two distinct conformations. Unlike previous findings showing that variable peptide conformations are caused only by the flexibility of the side chains in the groove, the skewing of the \u03b11 and \u03b12 helixes is important in the different peptide conformations in SLA-3*hs0202. We also determined the fundamental motif for SLA-3*hs0202 to be X-(M\/A\/R)-(N\/Q\/R\/F)-X-X-X-X-X-(V\/I) based on a series of structural and biochemical analyses, and 28 SLA-3*hs0202-restricted epitope candidates were identified from important IAV strains. We believe our structure and analyses of pSLA-3*hs0202 can benefit vaccine development to control IAV in swine.\n          <\/jats:p>","DOI":"10.1128\/jvi.00119-16","type":"journal-article","created":{"date-parts":[[2016,5,12]],"date-time":"2016-05-12T03:15:50Z","timestamp":1463022950000},"page":"6625-6641","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":39,"title":["Structural and Biochemical Analyses of Swine Major Histocompatibility Complex Class I Complexes and Prediction of the Epitope Map of Important Influenza A Virus Strains"],"prefix":"10.1128","volume":"90","author":[{"given":"Shuhua","family":"Fan","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing, People's Republic of China"},{"name":"College of Life Science and Agronomy, Zhoukou Normal University, Zhoukou, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanan","family":"Wu","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Song","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhenbao","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bo","family":"Jiang","sequence":"additional","affiliation":[{"name":"Department of Microbiology 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