Evidence map›Paper›PMID 31694937›Full record

ArticleJournal of virology2020

Mutations in Hypervariable Domain of Venezuelan Equine Encephalitis Virus nsP3 Protein Differentially Affect Viral Replication.

Chetan D Meshram, Aaron T Phillips, Tetyana Lukash, Nikita Shiliaev, Elena I Frolova, Ilya Frolov

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 12% 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, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Chetan D MeshramDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Aaron T PhillipsDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Tetyana LukashDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Nikita ShiliaevDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Elena I FrolovaDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.ORCID 0000-0001-6523-9336
Ilya FrolovDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA ivfrolov@uab.edu.ORCID 0000-0002-8548-2517
University of Alabama at Birmingham · US

Funding

Mechanistic role of ns2 protein in evasion of innate immune response by alphavirusesR01AI133159 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOVA, ELENA I · 2017 to 2021
$3.0M
Alphavirus nsP3 protein: roles of intrinsically disordered region in virus replication and pathogenesisR01AI118867 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOVA, ELENA I · 2015 to 2019
$1.8M
Mechanism of alphavirus packaging: designing of pseudoinfectious virusesR01AI095449 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOV, ILYA V. · 2012 to 2016
$1.8M
Mechanistic understanding of SH3 domain-containing protein function in alphavirus replicationR21AI146969 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOV, ILYA V. · 2019 to 2020
$401k
NIAID NIH HHS R01 AI095449NIAID NIH HHS R01 AI118867NIAID NIH HHS R01 AI133159NIAID NIH HHS R21 AI146969
6 · The paper itself

Abstract

Venezuelan equine encephalitis virus (VEEV) is one of the important human and animal pathogens. It forms replication enzyme complexes (RCs) containing viral nonstructural proteins (nsPs) that mediate the synthesis of virus-specific RNAs. The assembly and associated functions of RC also depend on the presence of a specific set of host proteins. Our study demonstrates that the hypervariable domain (HVD) of VEEV nsP3 interacts with the members of the FXR family of cellular proteins and also binds the Src homology 3 (SH3) domain-containing proteins CD2AP and SH3KBP1. Interactions with FXR family members are mediated by the C-terminal repeating peptide of HVD. A single short, minimal motif identified in this study is sufficient for driving efficient VEEV replication in the absence of HVD interactions with other host proteins. The SH3 domain-containing proteins bind to another fragment of VEEV HVD. They can promote viral replication in the absence of FXR-HVD interactions albeit less efficiently. VEEV replication can be also switched from an FXR-dependent to a chikungunya virus-specific, G3BP-dependent mode. The described modifications of VEEV HVD have a strong impact on viral replication

Indexed as

MutationProtein Interaction Domains and MotifsAdaptor Proteins, Signal TransducingAnimalsBinding SitesCell LineChikungunya virusCytoskeletal ProteinsDisease Models, AnimalEncephalitis Virus, Venezuelan EquineEncephalomyelitis, Venezuelan EquineHumansIntrinsically Disordered ProteinsMiceSequence Alignmentsrc Homology DomainsAdaptor Proteins, Signal TransducingCD2-associated proteinCytoskeletal ProteinsIntrinsically Disordered Proteinsnsp3 protein, alphavirusSh3kbp1 protein, mouseViral Nonstructural ProteinsalphavirusesCD2APFMRPFXR1FXR2intrinsically disordered proteinsnsP3SH3KBP1Venezuelan equine encephalitis virusviral pathogenesis

Identifiers

PMID31694937
PMCPMC7000987
OpenAlexW2985015632

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.