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dc.contributor.authorKraschnefski, Marken_US
dc.contributor.authorBugarcic, Andreaen_US
dc.contributor.authorE. Fleming, Fionaen_US
dc.contributor.authorYu, Xingen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.contributor.authorS. Coulson, Barbaraen_US
dc.contributor.authorBlanchard, Helenen_US
dc.date.accessioned2017-04-24T11:30:09Z
dc.date.available2017-04-24T11:30:09Z
dc.date.issued2009en_US
dc.date.modified2010-06-28T06:33:46Z
dc.identifier.issn14602423en_US
dc.identifier.doi10.1093/glycob/cwn119en_AU
dc.identifier.urihttp://hdl.handle.net/10072/29456
dc.description.abstractThe rotavirus spike protein VP4 mediates attachment to host cells and subsequent membrane penetration. The VP8* domain of VP4 forms the spike tips and is proposed to recognise host cell surface glycans. For sialidase-sensitive rotaviruses such as rhesus (RRV) this recognition involves terminal sialic acids. We show here that RRV VP8*64-224 protein competes with RRV infection of host cells, demonstrating its relevance to infection. In addition, we observe that the amino acids revealed by X-ray crystallography to be in direct contact with the bound sialic acid derivative methyl a-D-N-acetylneuraminide, and that are highly conserved amongst sialidase-sensitive rotaviruses, are residues that are also important in interactions with host-cell carbohydrates. Residues Arg101 and Ser190 of the RRV VP8* carbohydrate-binding site were mutated to assess their importance for binding to the sialic acid derivative and their competition with RRV infection of host cells. The crystallographic structure of the Arg101Ala mutant crystallised in the presence of sialic acid derivative was determined at 295 K to a resolution of 1.9 Ů Our multi-disciplinary study using X-ray crystallography, Saturation Transfer Difference nuclear magnetic resonance spectroscopy, isothermal titration calorimetry and competitive virus infectivity assays to investigate RRV wild-type and mutant VP8* proteins has provided the first evidence that the carbohydrate-binding cavity in RRV VP8* is used for host cell recognition, and this interaction is not only with the sialic acid portion but also other parts of the glycan structure.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherOxford University Pressen_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom194en_US
dc.relation.ispartofpageto200en_US
dc.relation.ispartofissue3en_US
dc.relation.ispartofjournalGlycobiologyen_US
dc.relation.ispartofvolume19en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchStructural Biology (incl. Macromolecular Modelling)en_US
dc.subject.fieldofresearchcode060112en_US
dc.titleEffects on sialic acid recognition of amino acid mutations in the carbohydrate-binding cleft of the rotavirus spike proteinen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2009
gro.hasfulltextNo Full Text


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