ArticleProceedings of the National Academy of Sciences of the United States of America2020
Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. 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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26 citing papers in PubMed, 46 citations in OpenAlex.
- Labeling and Localization Strategies for In Situ Cryo-Electron Tomography Across the Viral Life Cycle.Viruses · 2026Review
- Genetic complementation reveals structure-function links in nodavirus RNA replication complex crowns.PLoS pathogens · 2026Article
- Lipidomics reveals the pro-viral roles of ceramides during fish nodavirus infection.Journal of virology · 2026Article
- Nodavirus protein A's interdomain elbow controls RNA replication organelle formation and function.Nucleic acids research · 2026Article
- Cryo-electron tomography reveals coupled flavivirus replication, budding and maturation.Nature communications · 2026Article
- Cryo-electron tomography reveals coupled flavivirus replication, budding and maturation.bioRxiv : the preprint server for biology · 2024Article
- Positive-strand RNA virus genome replication organelles: structure, assembly, control.Trends in genetics : TIG · 2024Review
- Article
- SARS-CoV-2 nsp3 and nsp4 are minimal constituents of a pore spanning replication organelle.Nature communications · 2023Article
- Nodavirus RNA replication crown architecture reveals proto-crown precursor and viral protein A conformational switching.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Multifunctional Protein A Is the Only Viral Protein Required for Nodavirus RNA Replication Crown Formation.Viruses · 2022Article
- Molecular architecture of the Chikungunya virus replication complex.Science advances · 2022Article
- Article
- Article
- Adaptive Response ofJournal of fungi (Basel, Switzerland) · 2022Article
- High-resolution in situ structure determination by cryo-electron tomography and subtomogram averaging using emClarity.Nature protocols · 2022Review
- Cryo-electron tomography related radiation-damage parameters for individual-molecule 3D structure determination.Frontiers in chemistry · 2022Review
- Reinventing positive-strand RNA virus reverse genetics.Advances in virus research · 2022Article
- Cryo-electron microscopy of nodavirus RNA replication organelles illuminates positive-strand RNA virus genome replication.Current opinion in virology · 2021Review
- Ultrastructural Features of Membranous Replication Organelles Induced by Positive-Stranded RNA Viruses.Cells · 2021Review
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6 authors at 2 institutions in 1 country.
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Abstract
For positive-strand RNA [(+)RNA] viruses, the major target for antiviral therapies is genomic RNA replication, which occurs at poorly understood membrane-bound viral RNA replication complexes. Recent cryoelectron microscopy (cryo-EM) of nodavirus RNA replication complexes revealed that the viral double-stranded RNA replication template is coiled inside a 30- to 90-nm invagination of the outer mitochondrial membrane, whose necked aperture to the cytoplasm is gated by a 12-fold symmetric, 35-nm diameter "crown" complex that contains multifunctional viral RNA replication protein A. Here we report optimizing cryo-EM tomography and image processing to improve crown resolution from 33 to 8.5 Å. This resolves the crown into 12 distinct vertical segments, each with 3 major subdomains: A membrane-connected basal lobe and an apical lobe that together comprise the ∼19-nm-diameter central turret, and a leg emerging from the basal lobe that connects to the membrane at ∼35-nm diameter. Despite widely varying replication vesicle diameters, the resulting two rings of membrane interaction sites constrain the vesicle neck to a highly uniform shape. Labeling protein A with a His-tag that binds 5-nm Ni-nanogold allowed cryo-EM tomography mapping of the C terminus of protein A to the apical lobe, which correlates well with the predicted structure of the C-proximal polymerase domain of protein A. These and other results indicate that the crown contains 12 copies of protein A arranged basally to apically in an N-to-C orientation. Moreover, the apical polymerase localization has significant mechanistic implications for template RNA recruitment and (-) and (+)RNA synthesis.
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