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dc.contributor.authorBlanchard, Helenen_US
dc.contributor.authorYu, Xingen_US
dc.contributor.authorS. Coulson, Barbaraen_US
dc.contributor.authorvon Itzstein, Marken_US
dc.date.accessioned2017-05-03T14:15:09Z
dc.date.available2017-05-03T14:15:09Z
dc.date.issued2007en_US
dc.date.modified2009-01-13T07:12:13Z
dc.identifier.issn00222836en_US
dc.identifier.doi10.1016/j.jmb.2007.01.028en_AU
dc.identifier.urihttp://hdl.handle.net/10072/15645
dc.description.abstractRotavirus infection leads to the death of half a million children annually. The exact specifics of interaction between rotavirus particles and host cells enabling invasion and infection have remained elusive. Host cell oligosaccharides are critical components, and their involvement aids the virus in cell-recognition and attachment, as well as dictation of the remarkable host-specificity that rotaviruses demonstrate. Interaction between the rotavirus spike-protein carbohydrate-binding domain (VP8*) and cell surface oligosaccharides facilitate virus recognition of host-cells and attachment. Rotaviruses are considered, controversially, to recognise vastly different carbohydrate structures and either with incorporation of terminal sialic acid or without -as assessed by their ability to infect cells that have been pre-treated with sialidases. Herein, the X-ray crystallographic structures of VP8* from the sialidase insensitive Wa and the sialidase sensitive CRW-8 rotavirus strains that cause debilitating gastroenteritis in human and pig are reported. Striking differences are apparent regarding recognition of the sialic acid derivative methyl a-D-N-acetylneuraminide, presenting the first experimental evidence of the inability of the human rotavirus strain to bind this monosaccharide, that correlates with Wa and CRW-8 recognising sialidase-resistant and sialidase-sensitive receptors respectively. Identified are structural features that provide insight in attainment of substrate specificity exhibited by porcine strains as compared to rhesus rotavirus. Revealed in the CRW-8 VP8* structure is an additional bound ligand that intriguingly, is within a cleft located equivalent to the carbohydrate-binding region of galectins, and is suggestive of a new region for interaction with cell-surface carbohydrates. This novel result and detailed comparison of our representative sialidase-sensitive CRW-8 and insensitive Wa VP8* structures with those reported leads to our hypothesis that this groove is used for binding carbohydrates, and that for the human strains, as for other sialidase insensitive strains could represent a major oligosaccharide-binding region.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherAcademic Pressen_US
dc.publisher.placeUnited Kingdomen_US
dc.publisher.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/622890/description#descriptionen_AU
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom1215en_US
dc.relation.ispartofpageto1226en_US
dc.relation.ispartofjournalJournal of Molecular Biologyen_US
dc.relation.ispartofvolume367en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode250503en_US
dc.titleInsight into host cell carbohydrate-recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8*)en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightCopyright 2007 Elsevier. Please refer to the journal's website for access to the definitive, published version.en_AU
gro.date.issued2007
gro.hasfulltextNo Full Text


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