Files in this item
Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation
Item metadata
dc.contributor.author | Dong, Haohao | |
dc.contributor.author | Li, Ping | |
dc.contributor.author | Elliott, Richard M. | |
dc.contributor.author | Dong, Changjiang | |
dc.date.accessioned | 2014-08-26T10:31:01Z | |
dc.date.available | 2014-08-26T10:31:01Z | |
dc.date.issued | 2013-05 | |
dc.identifier | 63122078 | |
dc.identifier | 2776d0f9-fe35-49d9-a02b-6c9a05dcbb6c | |
dc.identifier | 000318155000025 | |
dc.identifier | 84877338947 | |
dc.identifier.citation | Dong , H , Li , P , Elliott , R M & Dong , C 2013 , ' Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation ' , Journal of Virology , vol. 87 , no. 10 , pp. 5593-5601 . https://doi.org/10.1128/JVI.00223-13 | en |
dc.identifier.issn | 0022-538X | |
dc.identifier.uri | https://hdl.handle.net/10023/5238 | |
dc.description | This work was supported by the Medical Research Council (grant no. G1100110/1 to C.D.) and the Wellcome Trust (career development fellowship WT083501MA to C.D. and program grant 079810 and project grant 091783 to R.M.E.). R.M.E. is a Wellcome Trust senior investigator. | en |
dc.description.abstract | Schmallenberg virus (SBV), a newly emerged orthobunyavirus (family Bunyaviridae), has spread rapidly across Europe and has caused congenital abnormalities in the offspring of cattle, sheep, and goats. Like other orthobunyaviruses, SBV contains a tripartite negative-sense RNA genome that encodes four structural and two nonstructural proteins. The nucleoprotein (N) encapsidates the three viral genomic RNA segments and plays a crucial role in viral RNA transcription and replication. Here we report the crystal structure of the bacterially expressed SBV nucleoprotein to a 3.06-angstrom resolution. The protomer is composed of two domains (N-terminal and C-terminal domains) with flexible N-terminal and C-terminal arms. The N protein has a novel fold and forms a central positively charged cleft for genomic RNA binding. The nucleoprotein purified under native conditions forms a tetramer, while the nucleoprotein obtained following denaturation and refolding forms a hexamer. Our structural and functional analyses demonstrate that both N-terminal and C-terminal arms are involved in N-N interaction and oligomerization and play an essential role in viral RNA synthesis, suggesting a novel mechanism for viral RNA encapsidation and transcription. | |
dc.format.extent | 9 | |
dc.format.extent | 4075555 | |
dc.language.iso | eng | |
dc.relation.ispartof | Journal of Virology | en |
dc.subject | Respiratory syncytial virus | en |
dc.subject | RNA complex | en |
dc.subject | Crystal-structure | en |
dc.subject | Reveals | en |
dc.subject | Europe | en |
dc.subject | Fever | en |
dc.subject | Crystallography | en |
dc.subject | Vectors | en |
dc.subject | Binding | en |
dc.subject | System | en |
dc.subject | QR355 Virology | en |
dc.subject.lcc | QR355 | en |
dc.title | Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation | 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 | 10.1128/JVI.00223-13 | |
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 |
This item appears in the following Collection(s)
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.