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dc.contributor.authorBowden, Thomas A.
dc.contributor.authorBitto, David
dc.contributor.authorMcLees, Angela
dc.contributor.authorYeromonahos, Christelle
dc.contributor.authorElliott, Richard M.
dc.contributor.authorHuiskonen, Juha T.
dc.date.accessioned2014-07-16T14:31:10Z
dc.date.available2014-07-16T14:31:10Z
dc.date.issued2013-05-16
dc.identifier.citationBowden , T A , Bitto , D , McLees , A , Yeromonahos , C , Elliott , R M & Huiskonen , J T 2013 , ' Orthobunyavirus ultrastructure and the curious tripodal glycoprotein spike ' , PLoS Pathogens , vol. 9 , no. 5 , e1003374 . https://doi.org/10.1371/journal.ppat.1003374en
dc.identifier.issn1553-7374
dc.identifier.otherPURE: 131417313
dc.identifier.otherPURE UUID: 7f100fe8-8b05-4c9e-a68d-02e3e267f7d3
dc.identifier.otherWOS: 000320032800047
dc.identifier.otherScopus: 84878490025
dc.identifier.urihttp://hdl.handle.net/10023/5031
dc.descriptionThis work was supported by the Wellcome Trust (090532/Z/09/Z; 089026/Z/09/Z to TAB; 079810 to RME) and by the Academy of Finland (130750 and 218080 to JTH).en
dc.description.abstractThe genus Orthobunyavirus within the family Bunyaviridae constitutes an expanding group of emerging viruses, which threaten human and animal health. Despite the medical importance, little is known about orthobunyavirus structure, a prerequisite for understanding virus assembly and entry. Here, using electron cryo-tomography, we report the ultrastructure of Bunyamwera virus, the prototypic member of this genus. Whilst Bunyamwera virions are pleomorphic in shape, they display a locally ordered lattice of glycoprotein spikes. Each spike protrudes 18 nm from the viral membrane and becomes disordered upon introduction to an acidic environment. Using sub-tomogram averaging, we derived a three-dimensional model of the trimeric pre-fusion glycoprotein spike to 3-nm resolution. The glycoprotein spike consists mainly of the putative class-II fusion glycoprotein and exhibits a unique tripod-like arrangement. Protein-protein contacts between neighbouring spikes occur at membrane-proximal regions and intra-spike contacts at membrane-distal regions. This trimeric assembly deviates from previously observed fusion glycoprotein arrangements, suggesting a greater than anticipated repertoire of viral fusion glycoprotein oligomerization. Our study provides evidence of a pH-dependent conformational change that occurs during orthobunyaviral entry into host cells and a blueprint for the structure of this group of emerging pathogens.
dc.format.extent10
dc.language.isoeng
dc.relation.ispartofPLoS Pathogensen
dc.rightsCopyright: © 2013 Bowden et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. http://creativecommons.org/licenses/by/3.0/en
dc.subjectLa-crosse-virusen
dc.subjectValley fever virusen
dc.subjectEM structure determinationen
dc.subjectMembrane-fusion proteinsen
dc.subjectElectron-microscopyen
dc.subjectCryoelectron tomographyen
dc.subjectEnvelope glycoproteinen
dc.subjectSchmallenberg virusen
dc.subjectOropouche virusen
dc.subjectUukuniemi virusen
dc.subjectQR355 Virologyen
dc.subject.lccQR355en
dc.titleOrthobunyavirus ultrastructure and the curious tripodal glycoprotein spikeen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1371/journal.ppat.1003374
dc.description.statusPeer revieweden


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