Evidence map›Paper›PMID 34372555›Full record

ReviewViruses2021

Viroplasms: Assembly and Functions of Rotavirus Replication Factories.

Guido Papa, Alexander Borodavka, Ulrich Desselberger

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.8field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 80 citations in OpenAlex.

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  11. Measuring the selective packaging of RNA molecules by viral coat proteins in cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Guido PapaMRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
Alexander BorodavkaDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.ORCID 0000-0002-5729-2687
Ulrich DesselbergerDepartment of Medicine, Addenbrooke's Hospital, University of Cambridge, Cambridge CB2 0QQ, UK.ORCID 0000-0003-0154-2410
University of Cambridge · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council U105181010Wellcome Trust 103068/Z/13/ZWellcome Trust 213437/Z/18/Z
6 · The paper itself

Abstract

Viroplasms are cytoplasmic, membraneless structures assembled in rotavirus (RV)-infected cells, which are intricately involved in viral replication. Two virus-encoded, non-structural proteins, NSP2 and NSP5, are the main drivers of viroplasm formation. The structures (as far as is known) and functions of these proteins are described. Recent studies using plasmid-only-based reverse genetics have significantly contributed to elucidation of the crucial roles of these proteins in RV replication. Thus, it has been recognized that viroplasms resemble liquid-like protein-RNA condensates that may be formed via liquid-liquid phase separation (LLPS) of NSP2 and NSP5 at the early stages of infection. Interactions between the RNA chaperone NSP2 and the multivalent, intrinsically disordered protein NSP5 result in their condensation (protein droplet formation), which plays a central role in viroplasm assembly. These droplets may provide a unique molecular environment for the establishment of inter-molecular contacts between the RV (+)ssRNA transcripts, followed by their assortment and equimolar packaging. Future efforts to improve our understanding of RV replication and genome assortment in viroplasms should focus on their complex molecular composition, which changes dynamically throughout the RV replication cycle, to support distinct stages of virion assembly.

Indexed as

AnimalsCapsid ProteinsCytoplasmCytosolHumansPhosphorylationRNA-Binding ProteinsRotavirusRotavirus InfectionsViral Nonstructural ProteinsViral Replication CompartmentsVirus AssemblyVirus ReplicationCapsid ProteinsNS35 protein, rotavirusNSP5 protein, rotavirus group ARNA-Binding ProteinsViral Nonstructural ProteinsCRISPR-Csy4 genome editingliquid-liquid phase separationNSP2NSP5protein-RNA condensatesreplication cyclereverse geneticsrotavirusviroplasm

Identifiers

PMID34372555
PMCPMC8310052
OpenAlexW3179164422

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.