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Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments
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dc.contributor.author | Barski, Michal | |
dc.contributor.author | Brennan, Benjamin | |
dc.contributor.author | Miller, Ona K. | |
dc.contributor.author | Potter, Jane A. | |
dc.contributor.author | Vijayakrishnan, Swetha | |
dc.contributor.author | Bhella, David | |
dc.contributor.author | Naismith, James H. | |
dc.contributor.author | Elliott, Richard M. | |
dc.contributor.author | Schwarz-Linek, Ulrich | |
dc.date.accessioned | 2017-09-22T08:30:16Z | |
dc.date.available | 2017-09-22T08:30:16Z | |
dc.date.issued | 2017-09-15 | |
dc.identifier.citation | Barski , M , Brennan , B , Miller , O K , Potter , J A , Vijayakrishnan , S , Bhella , D , Naismith , J H , Elliott , R M & Schwarz-Linek , U 2017 , ' Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments ' , eLife , vol. 6 , e29236 . https://doi.org/10.7554/eLife.29236 | en |
dc.identifier.issn | 2050-084X | |
dc.identifier.other | PURE: 250952162 | |
dc.identifier.other | PURE UUID: 95039784-fd90-4a68-a2a5-f8cefc64fd0a | |
dc.identifier.other | Scopus: 85029794182 | |
dc.identifier.other | ORCID: /0000-0003-0526-223X/work/40714974 | |
dc.identifier.other | WOS: 000410744900001 | |
dc.identifier.uri | https://hdl.handle.net/10023/11715 | |
dc.description.abstract | Rift Valley fever phlebovirus (RVFV) is a clinically and economically important pathogen increasingly likely to cause widespread epidemics. RVFV virulence depends on the interferon antagonist non-structural protein (NSs), which remains poorly characterized. We identified a stable core domain of RVFV NSs (residues 83-248), and solved its crystal structure, a novel all-helical fold organized into highly ordered fibrils. A hallmark of RVFV pathology is NSs filament formation in infected cell nuclei. Recombinant virus encoding the NSs core domain induced intranuclear filaments, suggesting it contains all essential determinants for nuclear translocation and filament formation. Mutations of key crystal fibril interface residues in viruses encoding full-length NSs completely abrogated intranuclear filament formation in infected cells. We propose the fibrillar arrangement of the NSs core domain in crystals reveals the molecular basis of assembly of this key virulence factor in cell nuclei. Our findings have important implications for fundamental understanding of RVFV virulence. | |
dc.format.extent | 20 | |
dc.language.iso | eng | |
dc.relation.ispartof | eLife | en |
dc.rights | Copyright Barski et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. | en |
dc.subject | Structural biology | en |
dc.subject | Virology | en |
dc.subject | X-ray crystallography | en |
dc.subject | Virulence factor | en |
dc.subject | Rift Valley fever virus | en |
dc.subject | QH301 Biology | en |
dc.subject | Biophysics | en |
dc.subject | Structural Biology | en |
dc.subject | Infectious Diseases | en |
dc.subject | DAS | en |
dc.subject | BDC | en |
dc.subject | R2C | en |
dc.subject | SDG 3 - Good Health and Well-being | en |
dc.subject.lcc | QH301 | en |
dc.title | Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | https://doi.org/10.7554/eLife.29236 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | 099220/Z/12/Z | en |
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