ArticleNucleic acids research2013
Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 83 citations in OpenAlex.
- Review
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- Schmallenberg virus epidemiology and regional control strategies: diagnostics, vaccines, and vector management.Frontiers in cellular and infection microbiology · 2025Review
- Using structure prediction of negative sense RNA virus nucleoproteins to assess evolutionary relationships.bioRxiv : the preprint server for biology · 2024Article
- Using structure prediction of negative sense RNA virus nucleoproteins to assess evolutionary relationships.Virus evolution · 2024Article
- Negative and ambisense RNA virus ribonucleocapsids: more than protective armor.Microbiology and molecular biology reviews : MMBR · 2023Review
- Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation.Science advances · 2023Article
- Isolation and characterization of Akabane virus Ib substrain and its pathogenesis in sulking mice.Virologica Sinica · 2023Article
- Organisation of the orthobunyavirus tripodal spike and the structural changes induced by low pH and KNature communications · 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
- Structural basis of IRGB10 oligomerization by GTP hydrolysis.Frontiers in immunology · 2023Article
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- A comprehensive list of the Bunyavirales replication promoters reveals a unique promoter structure in Nairoviridae differing from other virus families.Scientific reports · 2022Article
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- Structural insight into Marburg virus nucleoprotein-RNA complex formation.Nature communications · 2022Article
- Review
- A novel Schmallenberg virus subunit vaccine candidate protects IFNARScientific reports · 2020Article
- Mutagenic Analysis of Hazara Nairovirus Nontranslated Regions during Single- and Multistep Growth Identifies both Attenuating and Functionally Critical Sequences for Virus Replication.Journal of virology · 2020Article
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Authors and funding
17 authors at 4 institutions in 2 countries.
Funding
Abstract
All orthobunyaviruses possess three genome segments of single-stranded negative sense RNA that are encapsidated with the virus-encoded nucleocapsid (N) protein to form a ribonucleoprotein (RNP) complex, which is uncharacterized at high resolution. We report the crystal structure of both the Bunyamwera virus (BUNV) N-RNA complex and the unbound Schmallenberg virus (SBV) N protein, at resolutions of 3.20 and 2.75 Å, respectively. Both N proteins crystallized as ring-like tetramers and exhibit a high degree of structural similarity despite classification into different orthobunyavirus serogroups. The structures represent a new RNA-binding protein fold. BUNV N possesses a positively charged groove into which RNA is deeply sequestered, with the bases facing away from the solvent. This location is highly inaccessible, implying that RNA polymerization and other critical base pairing events in the virus life cycle require RNP disassembly. Mutational analysis of N protein supports a correlation between structure and function. Comparison between these crystal structures and electron microscopy images of both soluble tetramers and authentic RNPs suggests the N protein does not bind RNA as a repeating monomer; thus, it represents a newly described architecture for bunyavirus RNP assembly, with implications for many other segmented negative-strand RNA viruses.
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