Evidence map›Paper›PMID 24027337›Full record

ArticleJournal of virology2013

Identification of novel host factors via conserved domain search: Cns1 cochaperone is a novel restriction factor of tombusvirus replication in yeast.

Jing-Yi Lin, Peter D Nagy

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 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Contribution of yeast models to virus research.Applied microbiology and biotechnology · 2021
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
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

2 authors at 1 institution in 2 countries.

Jing-Yi LinDepartment of Plant Pathology, University of Kentucky, Lexington, Kentucky, USA.
Peter D Nagy
University of Kentucky · US

Funding

Mechanism of inhibition of RNA virus replication by host WW-domain proteinsR21AI109529 · NIAID · UNIVERSITY OF KENTUCKY · PI NAGY, PETER · 2014 to 2015
$385k
Mechanism of inhibition of +RNA virus replication by cyclophilinsR21AI096323 · NIAID · UNIVERSITY OF KENTUCKY · PI NAGY, PETER · 2011 to 2012
$378k
NIAID NIH HHS 5R21AI096323-02NIAID NIH HHS R21 AI096323NIAID NIH HHS R21 AI109529
6 · The paper itself

Abstract

A large number of host-encoded proteins affect the replication of plus-stranded RNA viruses by acting as susceptibility factors. Many other cellular proteins are known to function as restriction factors of viral infections. Previous studies with tomato bushy stunt tombusvirus (TBSV) in a yeast model host have revealed the inhibitory function of TPR (tetratricopeptide repeat) domain-containing cyclophilins, which are members of the large family of host prolyl isomerases, in TBSV replication. In this paper, we tested additional TPR-containing yeast proteins in a cell-free TBSV replication assay and identified the Cns1p cochaperone for heat shock protein 70 (Hsp70) and Hsp90 chaperones as a strong inhibitor of TBSV replication. Cns1p interacted with the viral replication proteins and inhibited the assembly of the viral replicase complex and viral RNA synthesis in vitro. Overexpression of Cns1p inhibited TBSV replication in yeast. The use of a temperature-sensitive (TS) mutant of Cns1p in yeast revealed that at a semipermissive temperature, TS Cns1p could not inhibit TBSV replication. Interestingly, Cns1p and the TPR-containing Cpr7p cyclophilin have similar inhibitory functions during TBSV replication, although some of the details of their viral restriction mechanisms are different. Our observations indicate that TPR-containing cellular proteins could act as virus restriction factors.

Indexed as

Virus ReplicationHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTombusvirusViral ProteinsCNS1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsViral Proteins

Identifiers

PMID24027337
PMCPMC3838133
OpenAlexW2056939106

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.