ArticleJournal of virology2013
Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 54 citations in OpenAlex.
- Review
- Structural Features of Nucleoproteins from the Recently DiscoveredInternational journal of molecular sciences · 2025Article
- The Phlebovirus Ribonucleoprotein: An Overview.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Virus as Teratogenic Agents.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Generation of Stable Cell Lines Expressing Akabane Virus N Protein and Insight into Its Function in Viral Replication.Pathogens (Basel, Switzerland) · 2023Article
- RNA Encapsulation Mode and Evolutionary Insights from the Crystal Structure of Emaravirus Nucleoprotein.Microbiology spectrum · 2023Article
- The mechanism of genome replication and transcription in bunyaviruses.PLoS pathogens · 2023Review
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- Observational Characterization of the Ecological and Environmental Features Associated with the Presence of Oropouche Virus and the Primary VectorTropical medicine and infectious disease · 2021Review
- Review
- Non-structural Proteins of Severe Fever With Thrombocytopenia Syndrome Virus Suppress RNA Synthesis in a Transcriptionally Active cDNA-Derived Viral RNA Synthesis System.Frontiers in microbiology · 2021Article
- A novel Schmallenberg virus subunit vaccine candidate protects IFNARScientific reports · 2020Article
- Brothers in Arms: Structure, Assembly and Function ofViruses · 2020Review
- Structural and functional similarities in bunyaviruses: Perspectives for pan-bunya antivirals.Reviews in medical virology · 2019Review
- Identification and localization of Tospovirus genus-wide conserved residues in 3D models of the nucleocapsid and the silencing suppressor proteins.Virology journal · 2019Article
- Mutational analysis of Rift Valley fever phlebovirus nucleocapsid protein indicates novel conserved, functional amino acids.PLoS neglected tropical diseases · 2017Article
- Distinct Mechanism for the Formation of the Ribonucleoprotein Complex of Tomato Spotted Wilt Virus.Journal of virology · 2017Article
- Asymmetric Trimeric Ring Structure of the Nucleocapsid Protein of Tospovirus.Journal of virology · 2017Article
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4 authors at 2 institutions in 1 country.
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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-Å 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.
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