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http://purl.uniprot.org/citations/23035213http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23035213http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23035213http://www.w3.org/2000/01/rdf-schema#comment"The rotavirus spike protein domain VP8* is essential for recognition of cell surface carbohydrate receptors, notably those incorporating N-acylneuraminic acids (members of the sialic acid family). N-Acetylneuraminic acids occur naturally in both animals and humans, whereas N-glycolylneuraminic acids are acquired only through dietary uptake in normal human tissues. The preference of animal rotaviruses for these natural N-acylneuraminic acids has not been comprehensively established, and detailed structural information regarding the interactions of different rotaviruses with N-glycolylneuraminic acids is lacking. In this study, distinct specificities of VP8* for N-acetyl- and N-glycolylneuraminic acids were revealed using biophysical techniques. VP8* protein from the porcine rotavirus CRW-8 and the bovine rotavirus Nebraska calf diarrhea virus (NCDV) showed a preference for N-glycolyl-over N-acetylneuraminic acids, in contrast to results obtained with rhesus rotavirus (RRV). Crystallographic structures of VP8* from CRW-8 and RRV with bound methyl-N-glycolylneuraminide revealed the atomic details of their interactions. We examined the influence of amino acid type at position 157, which is proximal to the ligand's N-acetyl or N-glycolyl moiety and can mutate upon cell culture adaptation. A structure-based hypothesis derived from these results could account for rotavirus discrimination between the N-acylneuraminic acid forms. Infectivity blockade experiments demonstrated that the determined carbohydrate specificities of these VP8* domains directly correlate with those of the corresponding infectious virus. This includes an association between CRW-8 adaption to cell culture, decreased competition by N-glycolylneuraminic acid for CRW-8 infectivity, and a Pro157-to-Ser157 mutation in VP8* that reduces binding affinity for N-glycolylneuraminic acid."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.org/dc/terms/identifier"doi:10.1128/jvi.06975-11"xsd:string
http://purl.uniprot.org/citations/23035213http://purl.org/dc/terms/identifier"doi:10.1128/jvi.06975-11"xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"von Itzstein M."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"von Itzstein M."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Blanchard H."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Blanchard H."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Coulson B.S."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Coulson B.S."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Dang V.T."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Dang V.T."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Fleming F.E."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/author"Fleming F.E."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/pages"13456-13466"xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/pages"13456-13466"xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/title"Structural basis of rotavirus strain preference toward N-acetyl- or N-glycolylneuraminic acid-containing receptors."xsd:string
http://purl.uniprot.org/citations/23035213http://purl.uniprot.org/core/title"Structural basis of rotavirus strain preference toward N-acetyl- or N-glycolylneuraminic acid-containing receptors."xsd:string
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