Evidence map›Paper›PMID 25329172›Full record

ArticlePLoS pathogens2014

Co-opted oxysterol-binding ORP and VAP proteins channel sterols to RNA virus replication sites via membrane contact sites.

Daniel Barajas, Kai Xu, Isabel Fernández de Castro Martín, Zsuzsanna Sasvari, Federica Brandizzi, Cristina Risco, Peter D Nagy

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
17.3field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Targeted knockout of a host peroxisomal peptidase confers field resistance to maize lethal necrosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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6 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Daniel BarajasDepartment of Plant Pathology, University of Kentucky, Lexington, Kentucky, United States of America.
Kai XuDepartment of Plant Pathology, University of Kentucky, Lexington, Kentucky, United States of America.
Isabel Fernández de Castro MartínCell Structure Laboratory, Centro Nacional de Biotecnología (CNB-CSIC), Campus de Cantoblanco, Madrid, Spain.
Zsuzsanna SasvariDepartment of Plant Pathology, University of Kentucky, Lexington, Kentucky, United States of America.
Federica BrandizziMSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan, United States of America.
Cristina RiscoCell Structure Laboratory, Centro Nacional de Biotecnología (CNB-CSIC), Campus de Cantoblanco, Madrid, Spain.
Peter D NagyDepartment of Plant Pathology, University of Kentucky, Lexington, Kentucky, United States of America.
University of Kentucky · USCentro Nacional de Biotecnología · ESMichigan United · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viruses recruit cellular membranes and subvert cellular proteins involved in lipid biosynthesis to build viral replicase complexes and replication organelles. Among the lipids, sterols are important components of membranes, affecting the shape and curvature of membranes. In this paper, the tombusvirus replication protein is shown to co-opt cellular Oxysterol-binding protein related proteins (ORPs), whose deletion in yeast model host leads to decreased tombusvirus replication. In addition, tombusviruses also subvert Scs2p VAP protein to facilitate the formation of membrane contact sites (MCSs), where membranes are juxtaposed, likely channeling lipids to the replication sites. In all, these events result in redistribution and enrichment of sterols at the sites of viral replication in yeast and plant cells. Using in vitro viral replication assay with artificial vesicles, we show stimulation of tombusvirus replication by sterols. Thus, co-opting cellular ORP and VAP proteins to form MCSs serves the virus need to generate abundant sterol-rich membrane surfaces for tombusvirus replication.

Indexed as

Virus ReplicationDNA ReplicationMitochondrial MembranesSaccharomyces cerevisiaeSterolsTombusvirusViral ProteinsSterolsViral Proteins

Identifiers

PMID25329172
PMCPMC4199759
OpenAlexW2089400774

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.