Evidence map›Paper›PMID 30021893›Full record

ArticleJournal of virology2018

The RNA-Binding Protein of a Double-Stranded RNA Virus Acts like a Scaffold Protein.

Carlos P Mata, Johann Mertens, Juan Fontana, Daniel Luque, Carolina Allende-Ballestero, David Reguera, Benes L Trus, Alasdair C Steven, José L Carrascosa, José R Castón

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

15 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
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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

10 authors at 5 institutions in 2 countries.

Carlos P MataDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, Madrid, Spain.
Johann MertensInstituto Madrileño de Estudios Avanzados en Nanociencia (IMDEA Nanociencia), Campus Cantoblanco, Madrid, Spain.
Juan FontanaLaboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.ORCID 0000-0002-9084-2927
Daniel LuqueDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, Madrid, Spain.
Carolina Allende-BallesteroDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, Madrid, Spain.
David RegueraDepartament de Física de la Matèria Condensada, Facultat de Física, Universitat de Barcelona, Barcelona, Spain.
Benes L TrusImaging Sciences Laboratory, CIT/NIH, Bethesda, Maryland, USA.
Alasdair C StevenLaboratory of Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA.
José L CarrascosaDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, Madrid, Spain jlcarras@cnb.csic.es jrcaston@cnb.csic.es.
José R CastónDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, Madrid, Spain jlcarras@cnb.csic.es jrcaston@cnb.csic.es.ORCID 0000-0003-2350-9048
Madrid Institute for Advanced Studies · ESCentro Nacional de Biotecnología · ESNational Institutes of Health · USInstituto de Salud Carlos III · ESUniversitat de Barcelona · ES

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
Biomedical ImagingZIACT000090 · CIT · CENTER FOR INFORMATION TECHNOLOGY · PI TRUS, BENES L · 2009 to 2018
$7.8M
6 · The paper itself

Abstract

Infectious bursal disease virus (IBDV), a nonenveloped, double-stranded RNA (dsRNA) virus with a T=13 icosahedral capsid, has a virion assembly strategy that initiates with a precursor particle based on an internal scaffold shell similar to that of tailed double-stranded DNA (dsDNA) viruses. In IBDV-infected cells, the assembly pathway results mainly in mature virions that package four dsRNA segments, although minor viral populations ranging from zero to three dsRNA segments also form. We used cryo-electron microscopy (cryo-EM), cryo-electron tomography, and atomic force microscopy to characterize these IBDV populations. The VP3 protein was found to act as a scaffold protein by building an irregular, ∼40-Å-thick internal shell without icosahedral symmetry, which facilitates formation of a precursor particle, the procapsid. Analysis of IBDV procapsid mechanical properties indicated a VP3 layer beneath the icosahedral shell, which increased the effective capsid thickness. Whereas scaffolding proteins are discharged in tailed dsDNA viruses, VP3 is a multifunctional protein. In mature virions, VP3 is bound to the dsRNA genome, which is organized as ribonucleoprotein complexes. IBDV is an amalgam of dsRNA viral ancestors and traits from dsDNA and single-stranded RNA (ssRNA) viruses.

Indexed as

Genome, ViralVirus AssemblyAnimalsBirnaviridae InfectionsCapsidCells, CulturedCoturnixCryoelectron MicroscopyInfectious bursal disease virusMuscle CellsRNA-Binding ProteinsRNA, Double-StrandedViral Structural ProteinsVirionRNA-Binding ProteinsRNA, Double-StrandedViral Structural ProteinsVP3 protein, infectious bursal disease viruscryo-EM and cryo-ETdsRNA-binding proteinIBDVscaffolding proteinvirus assembly

Identifiers

PMID30021893
PMCPMC6146815
OpenAlexW2883353754

What OpenQuestion holds

Textmetadata
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.