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dc.contributor.authorSingh, BK
dc.contributor.authorKoromyslova, A
dc.contributor.authorHansman, GS
dc.date.accessioned2021-08-18T03:55:54Z
dc.date.available2021-08-18T03:55:54Z
dc.date.issued2016
dc.identifier.issn1096-0341
dc.identifier.doi10.1016/j.virol.2015.10.022
dc.identifier.urihttp://hdl.handle.net/10072/407045
dc.description.abstractWe determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibody that was capable of binding the five different (GI-GV) P domains. Our data suggests that genetically diverse noroviruses still contain common epitopes.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherElsevier
dc.relation.ispartofpagefrom296
dc.relation.ispartofpageto301
dc.relation.ispartofjournalVirology
dc.relation.ispartofvolume487
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchHealth sciences
dc.subject.fieldofresearchAgricultural, veterinary and food sciences
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode3107
dc.subject.fieldofresearchcode42
dc.subject.fieldofresearchcode30
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsVirology
dc.subject.keywordsBovine norovirus
dc.subject.keywordsAntibodies
dc.titleStructural analysis of bovine norovirus protruding domain
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationSingh, BK; Koromyslova, A; Hansman, GS, Structural analysis of bovine norovirus protruding domain, Virology, 2016, 487, pp. 296-301
dcterms.dateAccepted2015-10-21
dc.date.updated2021-08-17T22:46:33Z
gro.hasfulltextNo Full Text
gro.griffith.authorHansman, Grant S.


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