Evidence map›Paper›PMID 20132841›Full record

ArticleJournal of virological methods2010

The use of AlphaLISA technology to detect interaction between hepatitis C virus-encoded NS5A and cyclophilin A.

Helen Waller, Udayan Chatterji, Philippe Gallay, Tanya Parkinson, Paul Targett-Adams

Abstract read
In one paragraph

Article in Journal of virological methods, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Induction of DUSP14 ubiquitination by PRMT5-mediated arginine methylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Chaperones in hepatitis C virus infection.World journal of hepatology · 2016
    Review
  12. Review
  13. Review
  14. Cyclophilin A as a New Therapeutic Target for Hepatitis C Virus-induced Hepatocellular Carcinoma.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2013
    Review
  15. Article
  16. HCV NS5A and IRF9 compete for CypA binding.Journal of hepatology · 2013
    Article
  17. Review
  18. Review
  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

5 authors at 2 institutions in 2 countries.

Helen WallerPfizer Global Research & Development, Antivirals Research Unit (IPC424), Sandwich Laboratories, Sandwich, Kent, CT13 9NJ, UK.
Udayan Chatterji
Philippe Gallay
Tanya Parkinson
Paul Targett-Adams
Pfizer (United Kingdom) · GBScripps Research Institute · US

Funding

Cyclophilins, Cyclophilin Inhibitors and Hepatitis CR01AI087746 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI GALLAY, PHILIPPE ANDRE · 2010 to 2014
$2.3M
NIAID NIH HHS R01 AI087746
6 · The paper itself

Abstract

Cyclosporine A (CsA) is an immunosuppressive molecule that also impedes replication of hepatitis C virus (HCV). CsA inhibits isomerase activity of cellular-encoded cyclophilin proteins, of which cyclophilin A (CypA) in particular is required for HCV replication. Evidence suggests that the HCV-encoded NS5A and NS5B proteins may govern dependence of the virus on CypA-mediated isomerase activity, although the molecular mechanisms involved are unclear. However, association of NS5A and NS5B, with CypA has been reported, raising the possibility that direct interaction between these proteins facilitates HCV replication. In the present study, mammalian two-hybrid and AlphaLISA technologies were utilized to detect interactions between NS5A and NS5B, with CypA. AlphaLISA analysis revealed associations between NS5A and CypA using purified proteins, and in cell lysates prepared from co-transfected cells. Importantly, the NS5A-CypA interactions were sensitive to CsA in a dose-responsive manner and an isomerase mutant of CypA interacted with NS5A less efficiently than wild-type CypA. These findings correlate the anti-HCV properties of CsA with an ability of the compound to disrupt NS5A-CypA interactions in vitro and in vivo, whilst providing the basis for development of assay platforms suitable to screen compound libraries for novel inhibitors of the NS5A-CypA interaction.

Indexed as

Two-Hybrid System TechniquesAnimalsCHO CellsCricetinaeCricetulusCyclophilin ACyclosporineDose-Response Relationship, DrugHepacivirusImmunosuppressive AgentsProtein BindingRecombinant ProteinsRNA-Dependent RNA PolymeraseTransfectionViral Nonstructural ProteinsCyclophilin ACyclosporineImmunosuppressive AgentsNS-5 protein, hepatitis C virusRecombinant ProteinsRNA-Dependent RNA PolymeraseViral Nonstructural Proteins

Identifiers

PMID20132841
PMCPMC6634308
OpenAlexW2060735361

What OpenQuestion holds

Textmetadata
LicenceTDM
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.