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Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein

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Item Type:Article
Title:Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein
Creators Name:Olal, D. and Dick, A. and Woods, V.L. and Liu, T. and Li, S. and Devignot, S. and Weber, F. and Saphire, E.O. and Daumke, O.
Abstract:Toscana virus is an emerging bunyavirus in Mediterranean Europe where it accounts for 80% of pediatric meningitis cases during the summer. The negative-strand ribonucleic acid (RNA) genome of the virus is wrapped around the virally encoded nucleoprotein N to form the ribonucleoprotein complex (RNP). We determined crystal structures of hexameric N alone (apo) and in complex with a nonameric single-stranded RNA. RNA is sequestered in a sequence-independent fashion in a deep groove inside the hexamer. At the junction between two adjacent copies of Ns, RNA binding induced an inter-subunit rotation, which opened the RNA-binding tunnel and created a new assembly interface at the outside of the hexamer. Based on these findings, we suggest a structural model for how binding of RNA to N promotes the formation of helical RNPs, which are a characteristic hallmark of many negative-strand RNA viruses.
Keywords:Binding Sites, Molecular Models, Nucleocapsid Proteins, Protein Binding, Protein Multimerization, Quaternary Protein Structure, Sandfly fever Naples virus, Secondary Protein Structure, Viral RNA, Virus Assembly, X-Ray Crystallography
Source:Nucleic Acids Research
Publisher:Oxford University Press
Page Range:6025-6037
Date:14 May 2014
Official Publication:https://doi.org/10.1093/nar/gku229
PubMed:View item in PubMed

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