Evidence map›Paper›PMID 24838241›Full record

ArticleThe Journal of biological chemistry2014

The association of hepatitis C virus glycoproteins with apolipoproteins E and B early in assembly is conserved in lipoviral particles.

Audrey Boyer, Amélie Dumans, Elodie Beaumont, Loïc Etienne, Philippe Roingeard, Jean-Christophe Meunier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.3field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Emerging role of lipophagy in liver disorders.Molecular and cellular biochemistry · 2024
    Review
  3. Apolipoprotein E and viral infection: Risks and Mechanisms.Molecular therapy. Nucleic acids · 2023
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. HCV Assembly and Egress via Modifications in Host Lipid Metabolic Systems.Cold Spring Harbor perspectives in medicine · 2021
    Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. The Role of ApoE in HCV Infection and Comorbidity.International journal of molecular sciences · 2019
    Review
  17. 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

6 authors at 1 institution in 1 country.

Audrey BoyerFrom the INSERM U966, Université François Rabelais and CHRU de Tours, 37032 Tours, France.
Amélie DumansFrom the INSERM U966, Université François Rabelais and CHRU de Tours, 37032 Tours, France.
Elodie BeaumontFrom the INSERM U966, Université François Rabelais and CHRU de Tours, 37032 Tours, France.
Loïc EtienneFrom the INSERM U966, Université François Rabelais and CHRU de Tours, 37032 Tours, France.
Philippe RoingeardFrom the INSERM U966, Université François Rabelais and CHRU de Tours, 37032 Tours, France.
Jean-Christophe MeunierFrom the INSERM U966, Université François Rabelais and CHRU de Tours, 37032 Tours, France Jean.meunier@univ-tours.fr.
Université de Tours · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In patients chronically infected with hepatitis C virus and in the HCV cell culture system (HCVcc), it is known that highly infectious virus particles have low to very low buoyant densities. These low densities have been attributed to the association of HCV with lipoprotein components, which occur during the viral morphogenesis. The resulting hybrid particles are known as lipoviral particles (LVP); however, very little is known about how these particles are created. In our study, we used Huh7.5 cells to investigate the intracellular association between envelope proteins and apolipoproteins B and E (ApoB and ApoE, respectively). In particular, we were interested in the role of this association in initiating LVP morphogenesis. Co-immunoprecipitation assays revealed that ApoB, ApoE, and HCV glycoproteins formed a protein complex early in the HCV lifecycle. Confocal analyses of naïve, E1E2-transduced and HCVcc-infected cells showed that HCV glycoproteins, ApoB and ApoE were found strongly colocalized only in the endoplasmic reticulum. We also found that HCV glycoproteins, ApoB and ApoE were already associated with intracellular infectious viral particles and, furthermore, that the protein complex was conserved in the infectious viral particles present in the supernatant of infected Huh7.5 cells. The association of HCV glycoproteins with ApoE was also evidenced in the HCVpp system, using the non-hepatic HEK293T cell line. We suggest that the complex formed by HCV E1E2, ApoB, and ApoE may initiate lipoviral particle morphogenesis.

Indexed as

Virus AssemblyApolipoproteins BApolipoproteins EEndoplasmic ReticulumHEK293 CellsHepacivirusHumansProtein BindingTime FactorsViral Envelope ProteinsVirionApolipoproteins BApolipoproteins EE1 protein, Hepatitis C virusglycoprotein E2, Hepatitis C virusViral Envelope ProteinsApolipoproteinGlycoproteinHepatitis C Virus (HCV)LipoproteinMorphogenesis

Identifiers

PMID24838241
PMCPMC4081931
OpenAlexW1982370923

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.