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


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.

SUBMITTER: Olal D 

PROVIDER: S-EPMC4027202 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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

Olal Daniel D   Dick Alexej A   Woods Virgil L VL   Liu Tong T   Li Sheng S   Devignot Stephanie S   Weber Friedemann F   Saphire Erica Ollmann EO   Daumke Oliver O  

Nucleic acids research 20140331 9


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 hexam  ...[more]

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