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Crystal structure of Schmallenberg orthobunyavirus nucleoprotein-RNA complex reveals a novel RNA sequestration mechanism
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dc.contributor.author | Dong, Haohao | |
dc.contributor.author | Li, Ping | |
dc.contributor.author | Boettcher, Bettina | |
dc.contributor.author | Elliott, Richard M. | |
dc.contributor.author | Dong, Changjiang | |
dc.date.accessioned | 2014-12-22T13:01:04Z | |
dc.date.available | 2014-12-22T13:01:04Z | |
dc.date.issued | 2013-08 | |
dc.identifier | 130824638 | |
dc.identifier | cbb63d50-e003-4ff4-958d-b24b08467594 | |
dc.identifier | 000321834600010 | |
dc.identifier | 84880692301 | |
dc.identifier.citation | Dong , 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.039057.113 | en |
dc.identifier.issn | 1355-8382 | |
dc.identifier.uri | https://hdl.handle.net/10023/5950 | |
dc.description.abstract | Schmallenberg 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.extent | 8 | |
dc.format.extent | 1562938 | |
dc.language.iso | eng | |
dc.relation.ispartof | RNA | en |
dc.subject | Schmallenberg virus | en |
dc.subject | orthobunyavirus | en |
dc.subject | bunyavirus | en |
dc.subject | nucleoprotein structure | en |
dc.subject | RNA replication and transcription | en |
dc.subject | Virus | en |
dc.subject | Encapsidation | en |
dc.subject | Europe | en |
dc.subject | Binding | en |
dc.subject | QR355 Virology | en |
dc.subject.lcc | QR355 | en |
dc.title | Crystal structure of Schmallenberg orthobunyavirus nucleoprotein-RNA complex reveals a novel RNA sequestration mechanism | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.sponsor | Medical Research Council | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.1261/rna.039057.113 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | 091783/Z/10/Z | en |
dc.identifier.grantnumber | 079810/Z/06/Z | en |
dc.identifier.grantnumber | G1100110 | en |
dc.identifier.grantnumber | 083501/Z/07/Z | en |
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