title: 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.
authors.affiliation: Max Delbrück Center for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA oliver.daumke@mdc-berlin.de.
authors.forename: Daniel
authors.initials: D
authors.lastname: Olal
authors.affiliation: Max Delbrück Center for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.
authors.forename: Alexej
authors.initials: A
authors.lastname: Dick
authors.affiliation: Department of Medicine, University of California at San Diego, La Jolla, CA 92093, USA.
authors.forename: Virgil L
authors.initials: VL
authors.lastname: Woods
authors.affiliation: Department of Medicine, University of California at San Diego, La Jolla, CA 92093, USA.
authors.forename: Tong
authors.initials: T
authors.lastname: Liu
authors.affiliation: Department of Medicine, University of California at San Diego, La Jolla, CA 92093, USA.
authors.forename: Sheng
authors.initials: S
authors.lastname: Li
authors.affiliation: Institute for Virology, Philipps-University Marburg, D-35043 Marburg, Germany.
authors.forename: Stephanie
authors.initials: S
authors.lastname: Devignot
authors.affiliation: Institute for Virology, Philipps-University Marburg, D-35043 Marburg, Germany.
authors.forename: Friedemann
authors.initials: F
authors.lastname: Weber
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: Erica Ollmann
authors.initials: EO
authors.lastname: Saphire
authors.affiliation: Max Delbrück Center for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany Freie Universität Berlin, Biochemistry, Takustrasse 6, 14195 Berlin, Germany oliver.daumke@mdc-berlin.de.
authors.forename: Oliver
authors.initials: O
authors.lastname: Daumke
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019590:Nucleocapsid Proteins / Q000737:chemistry*; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D012367:RNA, Viral / Q000737:chemistry*; D029301:Sandfly fever Naples virus / Q000502:physiology*; D019065:Virus Assembly
chemical_list: D019590:Nucleocapsid Proteins; D012367:RNA, Viral