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dc.contributor.authorDong, Haohao
dc.contributor.authorLi, Ping
dc.contributor.authorBoettcher, Bettina
dc.contributor.authorElliott, Richard M.
dc.contributor.authorDong, Changjiang
dc.date.accessioned2014-12-22T13:01:04Z
dc.date.available2014-12-22T13:01:04Z
dc.date.issued2013-08
dc.identifier.citationDong , H , Li , P , Boettcher , B , Elliott , R M & Dong , C 2013 , ' Crystal structure of Schmallenberg orthobunyavirus nucleoprotein-RNA complex reveals a novel RNA sequestration mechanism ' , RNA , vol. 19 , no. 8 , pp. 1129-1136 . https://doi.org/10.1261/rna.039057.113en
dc.identifier.issn1355-8382
dc.identifier.otherPURE: 130824638
dc.identifier.otherPURE UUID: cbb63d50-e003-4ff4-958d-b24b08467594
dc.identifier.otherWOS: 000321834600010
dc.identifier.otherScopus: 84880692301
dc.identifier.urihttp://hdl.handle.net/10023/5950
dc.description.abstractSchmallenberg virus (SBV) is a newly emerged orthobunyavirus (family Bunyaviridae) that has caused severe disease in the offspring of farm animals across Europe. Like all orthobunyaviruses, SBV contains a tripartite negative-sense RNA genome that is encapsidated by the viral nucleocapsid (N) protein in the form of a ribonucleoprotein complex (RNP). We recently reported the three-dimensional structure of SBV N that revealed a novel fold. Here we report the crystal structure of the SBV N protein in complex with a 42-nt-long RNA to 2.16 angstrom resolution. The complex comprises a tetramer of N that encapsidates the RNA as a cross-shape inside the protein ring structure, with each protomer bound to 11 ribonucleotides. Eight bases are bound in the positively charged cleft between the N- and C-terminal domains of N, and three bases are shielded by the extended N-terminal arm. SBV N appears to sequester RNA using a different mechanism compared with the nucleoproteins of other negative-sense RNA viruses. Furthermore, the structure suggests that RNA binding results in conformational changes of some residues in the RNA-binding cleft and the N- and C-terminal arms. Our results provide new insights into the novel mechanism of RNA encapsidation by orthobunyaviruses.
dc.format.extent8
dc.language.isoeng
dc.relation.ispartofRNAen
dc.rights© 2013; Published by Cold Spring Harbor Laboratory Press for the RNA Society. This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.en
dc.subjectSchmallenberg virusen
dc.subjectorthobunyavirusen
dc.subjectbunyavirusen
dc.subjectnucleoprotein structureen
dc.subjectRNA replication and transcriptionen
dc.subjectVirusen
dc.subjectEncapsidationen
dc.subjectEuropeen
dc.subjectBindingen
dc.subjectQR355 Virologyen
dc.subject.lccQR355en
dc.titleCrystal structure of Schmallenberg orthobunyavirus nucleoprotein-RNA complex reveals a novel RNA sequestration mechanismen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1261/rna.039057.113
dc.description.statusPeer revieweden


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