ArticleViruses2022
Multifunctional Protein A Is the Only Viral Protein Required for Nodavirus RNA Replication Crown Formation.
Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 10 citations in OpenAlex.
- Tuning intracellular immunity by Nodamura virus B2 protein enhances self-amplifying RNA activity.Nature communications · 2026Article
- Genetic complementation reveals structure-function links in nodavirus RNA replication complex crowns.PLoS pathogens · 2026Article
- Nodavirus protein A's interdomain elbow controls RNA replication organelle formation and function.Nucleic acids research · 2026Article
- Synthetic Peptides Suppress Nervous Necrosis Virus Absorption and Improve Survival Rates in European Sea Bass.Marine biotechnology (New York, N.Y.) · 2025Article
- Targeted protein degraders of SARS-CoV-2 Mpro are more active than enzymatic inhibition alone with activity against nirmatrelvir resistant virus.Communications medicine · 2025Article
- Positive-strand RNA virus genome replication organelles: structure, assembly, control.Trends in genetics : TIG · 2024Review
- SARS-CoV-2 nsp3 and nsp4 are minimal constituents of a pore spanning replication organelle.Nature communications · 2023Article
- Advances in Structural Virology via Cryo-EM in 2022.Viruses · 2023Article
- Structural and non-structural proteins in SARS-CoV-2: potential aspects to COVID-19 treatment or prevention of progression of related diseases.Cell communication and signaling : CCS · 2023Review
- 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
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Positive-strand RNA virus RNA genome replication occurs in membrane-associated RNA replication complexes (RCs). Nodavirus RCs are outer mitochondrial membrane invaginations whose necked openings to the cytosol are "crowned" by a 12-fold symmetrical proteinaceous ring that functions as the main engine of RNA replication. Similar protein crowns recently visualized at the openings of alphavirus and coronavirus RCs highlight their broad conservation and functional importance. Using cryo-EM tomography, we earlier showed that the major nodavirus crown constituent is viral protein A, whose polymerase, RNA capping, membrane interaction and multimerization domains drive RC formation and function. Other viral proteins are strong candidates for unassigned EM density in the crown. RNA-binding RNAi inhibitor protein B2 co-immunoprecipitates with protein A and could form crown subdomains that protect nascent viral RNA and dsRNA templates. Capsid protein may interact with the crown since nodavirus virion assembly has spatial and other links to RNA replication. Using cryoelectron tomography and complementary approaches, we show that, even when formed in mammalian cells, nodavirus RC crowns generated without B2 and capsid proteins are functional and structurally indistinguishable from mature crowns in infected
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