Evidence map›Paper›PMID 21248049›Full record

ArticleJournal of virology2011

Requirement for the amino-terminal domain of sindbis virus nsP4 during virus infection.

Jonathan C Rupp, Natasha Jundt, Richard W Hardy

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 22% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Infectomics of Chikungunya Virus: Roles Played by Host Factors.The American journal of tropical medicine and hygiene · 2025
    Review
  6. Article
  7. Molecular Virology of Chikungunya Virus.Current topics in microbiology and immunology · 2022
    Review
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  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
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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 1 institution in 1 country.

Jonathan C RuppDepartment of Biology, Indiana University, 216 S. Hawthorne Dr., Bloomington, Indiana 47405, USA.
Natasha Jundt
Richard W Hardy
Indiana University Bloomington · US

Funding

TRAINING IN GENETICST32GM007757 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI KUMAR, JUSTIN P · 1985 to 2014
$8.1M
NIGMS NIH HHS T32 GM007757NIGMS NIH HHS T32GM007757
6 · The paper itself

Abstract

The Sindbis virus RNA-dependent RNA polymerase nsP4 possesses an amino-terminal region that is unique to alphaviruses and is predicted to be disordered. To determine the importance of this region during alphavirus replication, 29 mutations were introduced, and resultant viruses were assessed for growth defects. Three small plaque mutants, D41A, G83L, and the triple mutant GPG((8-10))VAV, had defects in subgenome synthesis, minus-strand synthesis, and overall levels of viral RNA synthesis, respectively. Large plaque viruses were selected following passage in BHK-21 cells, and the genomes of these were sequenced. Suppressor mutations in nsP1, nsP2, and nsP3 that restored viral RNA synthesis were identified. An nsP2 change from M282 to L and an nsP3 change from H99 to N corrected the D41A-induced defect in subgenomic RNA synthesis. Three changes in nsP1, I351 to V, I388 to V, or the previously identified change, N374 to H (C. L. Fata, S. G. Sawicki, and D. L. Sawicki, J. Virol. 76:8641-8649, 2002), suppressed the minus-strand synthetic defect. A direct reversion back to G at position 8 reduced the RNA synthesis defect of the GPG((8-10))VAV virus. These results imply that nsP4's amino-terminal domain participates in distinct interactions with other nsPs in the context of differentially functioning RNA synthetic complexes, and flexibility in this domain is important for viral RNA synthesis. Additionally, the inability of the mutant viruses to efficiently inhibit host protein synthesis suggests a role for nsP4 in the regulation of host cell gene expression.

Indexed as

Virus ReplicationAmino Acid SubstitutionAnimalsCell LineCricetinaeDNA Mutational AnalysisMutant ProteinsMutation, MissenseProtein Structure, TertiarySindbis VirusSuppression, GeneticViral Nonstructural ProteinsViral Plaque AssayVirulence FactorsMutant ProteinsnsP4 protein, Sindbis virusViral Nonstructural ProteinsVirulence Factors

Identifiers

PMID21248049
PMCPMC3067876
OpenAlexW2140215972

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.