Evidence map›Paper›PMID 18495773›Full record

ArticleJournal of virology2008

Role for conserved residues of sindbis virus nonstructural protein 2 methyltransferase-like domain in regulation of minus-strand synthesis and development of cytopathic infection.

Mayuri, Todd W Geders, Janet L Smith, Richard J Kuhn

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Advances in COVID-19 mRNA vaccine development.Signal transduction and targeted therapy · 2022
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  3. Molecular Virology of Chikungunya Virus.Current topics in microbiology and immunology · 2022
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  17. Article
  18. Review
  19. Structural and functional insights into alphavirus polyprotein processing and pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. Article
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

4 authors at 2 institutions in 1 country.

MayuriMarkey Center for Structural Biology and Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
Todd W Geders
Janet L Smith
Richard J Kuhn
Purdue University West Lafayette · USUniversity of Michigan–Ann Arbor · US

Funding

Structure-function studies of alpha-and flavivirusesP01AI055672 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 2003 to 2010
$18.4M
NIAID NIH HHS AI55672NIAID NIH HHS P01 AI055672
6 · The paper itself

Abstract

The plus-strand RNA genome of Sindbis virus (SINV) encodes four nonstructural proteins (nsP1 to nsP4) that are involved in the replication of the viral RNA. The approximately 800-amino-acid nsP2 consists of an N-terminal domain with nucleoside triphosphatase and helicase activities and a C-terminal protease domain. Recently, the structure determined for Venezuelan equine encephalitis virus nsP2 indicated the presence of a previously unrecognized methyltransferase (MTase)-like domain within the C-terminal approximately 200 residues and raised a question about its functional importance. To assess the role of this MTase-like region in viral replication, highly conserved arginine and lysine residues were mutated to alanine. The plaque phenotypes of these mutants ranged from large/wild-type to small plaques with selected mutations demonstrating temperature sensitive lethality. The proteolytic polyprotein processing activity of nsP2 was unaffected in most of the mutants. Some of the temperature-sensitive mutants showed reduction in the minus-strand RNA synthesis, a function that has not yet been ascribed to nsP2. Mutation of SINV residue R615 rendered the virus noncytopathic and incapable of inhibiting the host cell translation but with no effects on the transcriptional inhibition. This property differentiated the mutation at R615 from previously described noncytopathic mutations. These results implicate nsP2 in regulation of minus-strand synthesis and suggest that different regions of the nsP2 MTase-like domain differentially modulate host defense mechanisms, independent of its role as the viral protease.

Indexed as

Virus ReplicationAmino Acid SubstitutionCysteine EndopeptidasesCytopathogenic Effect, ViralGenes, EssentialHot TemperatureMethyltransferasesModels, MolecularMutagenesis, Site-DirectedMutation, MissensePolyproteinsRNA, ViralSindbis VirusViral Plaque AssayViral ProteinsCysteine EndopeptidasesMethyltransferasesnsP2 proteinasePolyproteinsRNA, ViralViral Proteins

Identifiers

PMID18495773
PMCPMC2493352
OpenAlexW2122852718

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.