Evidence map›Paper›PMID 23015700›Full record

ArticleJournal of virology2012

Cytosolic phospholipase A2 gamma is involved in hepatitis C virus replication and assembly.

Song Xu, Rongjuan Pei, Min Guo, Qingxia Han, Juan Lai, Yun Wang, Chunchen Wu, Yuan Zhou, Mengji Lu, Xinwen Chen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. The Phospholipase AJournal of lipid and atherosclerosis · 2026
    Review
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  12. Review
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  15. What about COVID-19 and arachidonic acid pathway?European journal of clinical pharmacology · 2020
    Review
  16. Updating Phospholipase ABiomolecules · 2020
    Review
  17. Whole Lotta Lipids-from HCV RNA Replication to the Mature Viral Particle.International journal of molecular sciences · 2020
    Review
  18. Article
  19. 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

10 authors at 2 institutions in 2 countries.

Song XuState Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, People's Republic of China.
Rongjuan Pei
Min Guo
Qingxia Han
Juan Lai
Yun Wang
Chunchen Wu
Yuan Zhou
Mengji Lu
Xinwen Chen
Chinese Academy of Sciences · CNWuhan Institute of Virology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Similar to other positive-sense, single-stranded RNA viruses, hepatitis C virus (HCV) replicates its genome in a remodeled intracellular membranous structure known as the membranous web (MW). To date, the process of MW formation remains unclear. It is generally acknowledged that HCV nonstructural protein 4B (NS4B) can induce MW formation through interaction with the cytosolic endoplasmic reticulum (ER) membrane. Many host proteins, such as phosphatidylinositol 4-kinase IIIα (PI4KIIIα), have been identified as critical factors required for this process. We now report a new factor, the cytosolic phospholipase A2 gamma (PLA2G4C), which contributes to MW formation, HCV replication, and assembly. The PLA2G4C gene was identified as a host gene with upregulated expression upon HCV infection. Knockdown of PLA2G4C in HCV-infected cells or HCV replicon-containing cells by small interfering RNA (siRNA) significantly suppressed HCV replication and assembly. In addition, the chemical inhibitor methyl arachidonyl fluorophosphonate (MAFP), which specifically inhibits PLA2, reduced HCV replication and assembly. Electron microscopy demonstrated that MW structure formation was defective after PLA2G4C knockdown in HCV replicon-containing cells. Further analysis by immunostaining and immunoprecipitation assays indicated that PLA2G4C colocalized with the HCV proteins NS4B and NS5A in cells infected with JFH-1 and interacted with NS4B. In addition, PLA2G4C was able to transport the HCV nonstructural proteins from replication sites to lipid droplets, the site for HCV assembly. These data suggest that PLA2G4C plays an important role in the HCV life cycle and might represent a potential target for anti-HCV therapy.

Indexed as

Arachidonic AcidArachidonic AcidsBlotting, WesternCell LineCytosolDNA PrimersEndoplasmic ReticulumGene Knockdown TechniquesGroup IV Phospholipases A2HepacivirusHumansImmunoprecipitationMicroscopy, FluorescenceOrganophosphonatesPlasmidsReal-Time Polymerase Chain ReactionArachidonic AcidArachidonic AcidsDNA PrimersGroup IV Phospholipases A2methyl arachidonylfluorophosphonateNS4B protein, flavivirusOrganophosphonatesRNA, Small InterferingViral Nonstructural Proteins

Identifiers

PMID23015700
PMCPMC3497680
OpenAlexW2131866222

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.