Evidence map›Paper›PMID 20668085›Full record

ArticleJournal of virology2010

A new cistron in the murine hepatitis virus replicase gene.

Helen L Stokes, Surendranath Baliji, Chang Guo Hui, Stanley G Sawicki, Susan C Baker, Stuart G Siddell

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 23 citations in OpenAlex.

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  4. Physico-Chemical Mechanisms of the Functioning of Membrane-Active Proteins of Enveloped Viruses.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022
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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 4 institutions in 2 countries.

Helen L StokesDepartment of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, UK.
Surendranath Baliji
Chang Guo Hui
Stanley G Sawicki
Susan C Baker
Stuart G Siddell
University of Bristol · GBLoyola University Chicago · USUniversity of Chicago · USUniversity of Toledo Medical Center · US

Funding

Protein Expression and PurificationP01AI060915 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI JOHNSON, MICHAEL E. · 2005 to 2009
$7.7M
NIAID NIH HHS AI 060915NIAID NIH HHS P01 AI060915Wellcome TrustWellcome Trust 06548
6 · The paper itself

Abstract

We report an RNA-negative, temperature-sensitive (ts) mutant of Murine hepatitis virus, Bristol ts31 (MHV-Brts31), that defines a new complementation group within the MHV replicase gene locus. MHV-Brts31 has near-normal levels of RNA synthesis at the permissive temperature of 33 degrees C but is unable to synthesize viral RNA when the infection is initiated and maintained at the nonpermissive temperature of 39.5 degrees C. Sequence analysis of MHV-Brts31 RNA indicated that a single G-to-A transition at codon 1307 in open reading frame 1a, which results in a replacement of methionine-475 with isoleucine in nonstructural protein 3 (nsp3), was responsible for the ts phenotype. This conclusion was confirmed using a vaccinia virus-based reverse genetics system to produce a recombinant virus, Bristol tsc31 (MHV-Brtsc31), which has the same RNA-negative ts phenotype and complementation profile as those of MHV-Brts31. The analysis of protein synthesis in virus-infected cells showed that, at the nonpermissive temperature, MHV-Brtsc31 was not able to proteolytically process either p150, the precursor polypeptide of the replicase nonstructural proteins nsp4 to nsp10, or the replicase polyprotein pp1ab to produce nsp12. The processing of replicase polyprotein pp1a in the region of nsp1 to nsp3 was not affected. Transmission electron microscopy showed that, compared to revertant virus, the number of double-membrane vesicles in MHV-Brts31-infected cells is reduced at the nonpermissive temperature. These results identify a new cistron in the MHV replicase gene locus and show that nsp3 has an essential role in the assembly of a functional MHV replication-transcription complex.

Indexed as

Genes, ViralAnimalsCell LineGenetic Complementation TestHeLa CellsHumansMiceMicroscopy, Electron, TransmissionMurine hepatitis virusMutationPhenotypeProtein Processing, Post-TranslationalRNA-Dependent RNA PolymeraseRNA, ViralTemperatureViral ProteinsRNA-Dependent RNA PolymeraseRNA, ViralViral Proteins

Identifiers

PMID20668085
PMCPMC2937787
OpenAlexW2133269779

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.