Evidence map›Paper›PMID 23637407›Full record

ArticleJournal of virology2013

Hypervariable domain of nonstructural protein nsP3 of Venezuelan equine encephalitis virus determines cell-specific mode of virus replication.

Niall J Foy, Maryna Akhrymuk, Alexander V Shustov, Elena I Frolova, Ilya Frolov

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 11% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Pooled it
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  11. Molecular Virology of Chikungunya Virus.Current topics in microbiology and immunology · 2022
    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

5 authors at 1 institution in 1 country.

Niall J FoyDepartment of Microbiology, University of Alabama, Birmingham, Alabama, USA.
Maryna Akhrymuk
Alexander V Shustov
Elena I Frolova
Ilya Frolov
University of Alabama at Birmingham · US

Funding

Mechanism of alphavirus packaging: designing of pseudoinfectious virusesR01AI095449 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOV, ILYA V. · 2012 to 2016
$1.8M
The Molecular Basis of VEEV PathogenesisR01AI070207 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI FROLOV, ILYA V. · 2008 to 2012
$1.6M
Sindbis nonstructural protein nsP2: Interaction with cellular proteinsR01AI073301 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI FROLOVA, ELENA I · 2008 to 2012
$1.6M
Multiple functions of VEEV nsP3 in virus replicationR56AI091705 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOVA, ELENA I · 2011 to 2011
$366k
NIAID NIH HHS R01 AI070207NIAID NIH HHS R01AI070207NIAID NIH HHS R01 AI073301NIAID NIH HHS R01AI073301NIAID NIH HHS R01 AI095449NIAID NIH HHS R01AI095449NIAID NIH HHS R56 AI091705NIAID NIH HHS R56AI091705
6 · The paper itself

Abstract

Venezuelan equine encephalitis virus (VEEV) is one of the most pathogenic members of the Alphavirus genus in the Togaviridae family. This genus is divided into the Old World and New World alphaviruses, which demonstrate profound differences in pathogenesis, replication, and virus-host interactions. VEEV is a representative member of the New World alphaviruses. The biology of this virus is still insufficiently understood, particularly the function of its nonstructural proteins in RNA replication and modification of the intracellular environment. One of these nonstructural proteins, nsP3, contains a hypervariable domain (HVD), which demonstrates very low overall similarity between different alphaviruses, suggesting the possibility of its function in virus adaptation to different hosts and vectors. The results of our study demonstrate the following. (i) Phosphorylation of the VEEV nsP3-specific HVD does not play a critical role in virus replication in cells of vertebrate origin but is important for virus replication in mosquito cells. (ii) The VEEV HVD is not required for viral RNA replication in the highly permissive BHK-21 cell line. In fact, it can be either completely deleted or replaced by a heterologous protein sequence. These variants require only one or two additional adaptive mutations in nsP3 and/or nsP2 proteins to achieve an efficiently replicating phenotype. (iii) However, the carboxy-terminal repeat in the VEEV HVD is indispensable for VEEV replication in the cell lines other than BHK-21 and plays a critical role in formation of VEEV-specific cytoplasmic protein complexes. Natural VEEV variants retain at least one of the repeated elements in their nsP3 HVDs.

Indexed as

Genetic VariationAmino Acid SequenceAnimalsAntibodies, MonoclonalCricetinaeCulicidaeElectroporationEncephalitis Virus, Venezuelan EquineFluorescent Antibody TechniqueMiceMicroscopy, ConfocalMolecular Sequence DataNIH 3T3 CellsPhosphorylationPlasmidsProtein Structure, TertiaryAntibodies, Monoclonalnsp3 protein, alphavirusViral Nonstructural Proteins

Identifiers

PMID23637407
PMCPMC3700263
OpenAlexW1989720516

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.