Evidence map›Paper›PMID 24169621›Full record

ArticleMolecular & cellular proteomics : MCP2014

Elucidating novel hepatitis C virus-host interactions using combined mass spectrometry and functional genomics approaches.

Marie-Anne Germain, Laurent Chatel-Chaix, Bridget Gagné, Éric Bonneil, Pierre Thibault, Fabrine Pradezynski, Benoît de Chassey, Laurène Meyniel-Schicklin, Vincent Lotteau, Martin Baril and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. 1,25-Dihydroxyvitamin DInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. MASS SPECTROMETRY IN VIROLOGICAL SCIENCES.Mass spectrometry reviews · 2020
    Review
  15. Article
  16. The exocyst complex regulates insulin-stimulated glucose uptake of skeletal muscle cells.American journal of physiology. Endocrinology and metabolism · 2019
    Article
  17. Article
  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

11 authors at 2 institutions in 2 countries.

Marie-Anne GermainInstitut de Recherche en Immunologie et en Cancérologie (IRIC), Université de Montréal, C.P. 6128, succursale Centre-ville, Montréal, Québec H3C 3J7, Canada;
Laurent Chatel-Chaix
Bridget Gagné
Éric Bonneil
Pierre Thibault
Fabrine Pradezynski
Benoît de Chassey
Laurène Meyniel-Schicklin
Vincent Lotteau
Martin Baril
Daniel Lamarre
Institute for Research in Immunology and Cancer · CAUniversité Claude Bernard Lyon 1 · FR

Funding

Canadian Institutes of Health Research MOP-115058
6 · The paper itself

Abstract

More than 170 million people worldwide are infected with the hepatitis C virus (HCV), for which future therapies are expected to rely upon a combination of oral antivirals. For a rapidly evolving virus like HCV, host-targeting antivirals are an attractive option. To decipher the role of novel HCV-host interactions, we used a proteomics approach combining immunoprecipitation of viral-host protein complexes coupled to mass spectrometry identification and functional genomics RNA interference screening of HCV partners. Here, we report the proteomics analyses of protein complexes associated with Core, NS2, NS3/4A, NS4B, NS5A, and NS5B proteins. We identified a stringent set of 98 human proteins interacting specifically with one of the viral proteins. The overlap with previous virus-host interaction studies demonstrates 24.5% shared HCV interactors overall (24/98), illustrating the reliability of the approach. The identified human proteins show enriched Gene Ontology terms associated with the endoplasmic reticulum, transport proteins with a major contribution of NS3/4A interactors, and transmembrane proteins for Core interactors. The interaction network emphasizes a high degree distribution, a high betweenness distribution, and high interconnectivity of targeted human proteins, in agreement with previous virus-host interactome studies. The set of HCV interactors also shows extensive enrichment for known targets of other viruses. The combined proteomic and gene silencing study revealed strong enrichment in modulators of HCV RNA replication, with the identification of 11 novel cofactors among our set of specific HCV partners. Finally, we report a novel immune evasion mechanism of NS3/4A protein based on its ability to affect nucleocytoplasmic transport of type I interferon-mediated signal transducer and activator of transcription 1 nuclear translocation. The study revealed highly stringent association between HCV interactors and their functional contribution to the viral replication cycle and pathogenesis.

Indexed as

ProteomicsGenomicsHepacivirusHost-Pathogen InteractionsHumansMass SpectrometryMembrane ProteinsRNA InterferenceViral ProteinsMembrane ProteinsViral Proteins

Identifiers

PMID24169621
PMCPMC3879614
OpenAlexW2124927273

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.