Evidence map›Paper›PMID 26336920›Full record

ArticleScientific reports2015

A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability.

Johann Mertens, Santiago Casado, Carlos P Mata, Mercedes Hernando-Pérez, Pedro J de Pablo, José L Carrascosa, José R Castón

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  17. TensorCalculator: exploring the evolution of mechanical stress in the CCMV capsid.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  18. Assembly/disassembly of a complex icosahedral virus to incorporate heterologous nucleic acids.Journal of physics. Condensed matter : an Institute of Physics journal · 2017
    Article
  19. Review
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

7 authors at 3 institutions in 1 country.

Johann MertensInstituto Madrileño de Estudios Avanzados en Nanociencia (IMDEA Nanociencia) Campus Cantoblanco, 28049 Madrid, Spain.
Santiago CasadoInstituto Madrileño de Estudios Avanzados en Nanociencia (IMDEA Nanociencia) Campus Cantoblanco, 28049 Madrid, Spain.
Carlos P MataDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología/CSIC, Campus Cantoblanco, 28049 Madrid, Spain.
Mercedes Hernando-PérezDepartamento de Física de la Materia Condensada C03, Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Pedro J de PabloDepartamento de Física de la Materia Condensada C03, Universidad Autónoma de Madrid, 28049 Madrid, Spain.
José L CarrascosaUnidad Asociada de Nanobiotecnología CNB-CSIC-IMDEA, Cantoblanco, E-28049 Madrid, Spain.
José R CastónUnidad Asociada de Nanobiotecnología CNB-CSIC-IMDEA, Cantoblanco, E-28049 Madrid, Spain.
Centro Nacional de Biotecnología · ESMadrid Institute for Advanced Studies · ESUniversidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viral capsids are metastable structures that perform many essential processes; they also act as robust cages during the extracellular phase. Viruses can use multifunctional proteins to optimize resources (e.g., VP3 in avian infectious bursal disease virus, IBDV). The IBDV genome is organized as ribonucleoproteins (RNP) of dsRNA with VP3, which also acts as a scaffold during capsid assembly. We characterized mechanical properties of IBDV populations with different RNP content (ranging from none to four RNP). The IBDV population with the greatest RNP number (and best fitness) showed greatest capsid rigidity. When bound to dsRNA, VP3 reinforces virus stiffness. These contacts involve interactions with capsid structural subunits that differ from the initial interactions during capsid assembly. Our results suggest that RNP dimers are the basic stabilization units of the virion, provide better understanding of multifunctional proteins, and highlight the duality of RNP as capsid-stabilizing and genetic information platforms.

Indexed as

Binding SitesBirnaviridaeCapsidElastic ModulusProtein BindingRibonucleoproteinsRNA, ViralStress, MechanicalTensile StrengthRibonucleoproteinsRNA, Viral

Identifiers

PMID26336920
PMCPMC4559658
OpenAlexW1238100503

What OpenQuestion holds

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LicenceCC BY
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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.