ArticleJournal of virology2011
Rotavirus VP2 core shell regions critical for viral polymerase activation.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Single-round infectious rotaviruses with deletions of VP7 or VP4 genes, based on SA11 and WC3 strain backbones, and their potential use as viral vectors.PLoS pathogens · 2025Article
- Rotavirus Infections: Pathophysiology, Symptoms, and Vaccination.Pathogens (Basel, Switzerland) · 2025Review
- Characterization of viroplasm-like structures by co-expression of NSP5 and NSP2 across rotavirus species A to J.Journal of virology · 2024Article
- Generation of single-round infectious rotavirus with a mutation in the intermediate capsid protein VP6.Journal of virology · 2024Article
- Review
- Review
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- In vitro particle-associated uridyltransferase activity of the rotavirus VP1 polymerase.Virology · 2022Article
- Evolutionary changes between pre- and post-vaccine South African group A G2P[4] rotavirus strains, 2003-2017.Microbial genomics · 2022Article
- Reverse genetic engineering of simian rotaviruses with temperature-sensitive lesions in VP1, VP2, and VP6.Virus research · 2021Article
- Review
- Identification of a Ruminant Origin Group B Rotavirus Associated with Diarrhea Outbreaks in Foals.Viruses · 2021Article
- Asymmetric reconstruction of mammalian reovirus reveals interactions among RNA, transcriptional factor µ2 and capsid proteins.Nature communications · 2021Article
- Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.Journal of virology · 2020Article
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Coding-Gene Coevolution Analysis of Rotavirus Proteins: A Bioinformatics and Statistical Approach.Genes · 2019Article
- Article
- Group A Rotavirus VP1 Polymerase and VP2 Core Shell Proteins: Intergenotypic Sequence Variation andJournal of virology · 2019Article
- Cryo-EM Reveals Architectural Diversity in Active Rotavirus Particles.Computational and structural biotechnology journal · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The innermost VP2 core shell of the triple-layered, icosahedral rotavirus particle surrounds the viral genome and RNA processing enzymes, including the RNA-dependent RNA polymerase (VP1). In addition to anchoring VP1 within the core, VP2 is also an essential cofactor that triggers the polymerase to initiate double-stranded RNA (dsRNA) synthesis using packaged plus-strand RNA templates. The VP2 requirement effectively couples packaging with genome replication and ensures that VP1 makes dsRNA only within an assembling previrion particle. However, the mechanism by which the rotavirus core shell protein activates the viral polymerase remains very poorly understood. In the current study, we sought to elucidate VP2 regions critical for VP1-mediated in vitro dsRNA synthesis. By comparing the functions of proteins from several different rotaviruses, we found that polymerase activation by the core shell protein is specific. Through truncation and chimera mutagenesis, we demonstrate that the VP2 amino terminus, which forms a decameric, internal hub underneath each 5-fold axis, plays an important but nonspecific role in VP1 activation. Our results indicate that the VP2 residues correlating with polymerase activation specificity are located on the inner face of the core shell, distinct from the amino terminus. Based on these findings, we predict that several regions of VP2 engage the polymerase during the concerted processes of rotavirus core assembly and genome replication.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.