ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structure of RNA polymerase complex and genome within a dsRNA virus provides insights into the mechanisms of transcription and assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
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- Liquid-liquid phase separation is essential for reovirus viroplasm formation and immune evasion.Journal of virology · 2024Article
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- Sequences at gene segment termini inclusive of untranslated regions and partial open reading frames play a critical role in mammalian orthoreovirus S gene packaging.PLoS pathogens · 2024Article
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- Asymmetric reconstruction of the aquareovirus core at near-atomic resolution and mechanism of transcription initiation.Protein & cell · 2023Article
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- Grass Carp Reovirus Induces Formation of Lipid Droplets as Sites for Its Replication and Assembly.mBio · 2022Article
- In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly.Communications biology · 2022Article
- Molecular Characterization of Outer Capsid Proteins VP5 and VP7 of Grass Carp Reovirus.Viruses · 2022Article
- Viral Capsid and Polymerase in Reoviridae.Sub-cellular biochemistry · 2022Article
- Cryo-electron microscopy of nodavirus RNA replication organelles illuminates positive-strand RNA virus genome replication.Current opinion in virology · 2021Review
- The reovirus μ2 C-terminal loop inversely regulates NTPase and transcription functions versus binding to factory-forming μNS and promotes replication in tumorigenic cells.Journal of virology · 2021Article
- Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Reoviridae transcription is more than an open-and-shut case.Nature structural & molecular biology · 2019Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most double-stranded RNA (dsRNA) viruses transcribe RNA plus strands within a common innermost capsid shell. This process requires coordinated efforts by RNA-dependent RNA polymerase (RdRp) together with other capsid proteins and genomic RNA. Here we report the near-atomic resolution structure of the RdRp protein VP2 in complex with its cofactor protein VP4 and genomic RNA within an aquareovirus capsid using 200-kV cryoelectron microscopy and symmetry-mismatch reconstruction. The structure of these capsid proteins enabled us to observe the elaborate nonicosahedral structure within the double-layered icosahedral capsid. Our structure shows that the RdRp complex is anchored at the inner surface of the capsid shell and interacts with genomic dsRNA and four of the five asymmetrically arranged N termini of the capsid shell proteins under the fivefold axis, implying roles for these N termini in virus assembly. The binding site of the RNA end at VP2 is different from the RNA cap binding site identified in the crystal structure of orthoreovirus RdRp λ3, although the structures of VP2 and λ3 are almost identical. A loop, which was thought to separate the RNA template and transcript, interacts with an apical domain of the capsid shell protein, suggesting a mechanism for regulating RdRp replication and transcription. A conserved nucleoside triphosphate binding site was localized in our RdRp cofactor protein VP4 structure, and interactions between the VP4 and the genomic RNA were identified.
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