Evidence map›Paper›PMID 24797426›Full record

ArticleMolecular & cellular proteomics : MCP2014

The intraviral protein interaction network of hepatitis C virus.

Nicole Hagen, Karen Bayer, Kathrin Rösch, Michael Schindler

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. AlphaFold Prediction of Protein-Protein Interactions in theInternational journal of molecular sciences · 2025
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  7. Analysis of IFITM-IFITM Interactions by a Flow Cytometry-Based FRET Assay.International journal of molecular sciences · 2019
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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

4 authors at 2 institutions in 1 country.

Nicole HagenFrom the ‡Heinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, Germany;
Karen Bayer¶Institute of Virology, Helmholtz Zentrum Munich, German Research Center for Environmental Health, 85764 Neuherberg, Germany;
Kathrin RöschFrom the ‡Heinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, Germany;
Michael SchindlerFrom the ‡Heinrich Pette Institute, Leibniz Institute for Experimental Virology, 20251 Hamburg, Germany; ¶Institute of Virology, Helmholtz Zentrum Munich, German Research Center for Environmental Health, 85764 Neuherberg, Germany; ‖Institute of Medical Virology and Epidemiology of Viral Diseases, University Clinic Tübingen, 72076 Tübingen, Germany michael.schindler@helmholtz-muenchen.de.
Helmholtz Zentrum München · DELeibniz Institute of Virology (LIV) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatitis C virus (HCV) is a global health problem and one of the main reasons for chronic liver diseases such as cirrhosis and hepatocellular carcinoma. The HCV genome is translated into a polyprotein which is proteolytically processed into 10 viral proteins. The interactome of the HCV proteins with the host cell has been worked out; however, it remains unclear how viral proteins interact with each other. We aimed to generate the interaction network of these 10 HCV proteins using a flow-cytometry-based FRET assay established in our laboratory (Banning, C., Votteler, J., Hoffmann, D., Koppensteiner, H., Warmer, M., Reimer, R., Kirchhoff, F., Schubert, U., Hauber, J., and Schindler, M. (2010) A flow cytometry-based FRET assay to identify and analyse protein-protein interactions in living cells. PLoS One 5, e9344). HCV proteins were constructed as fusions with the chromophores CFP and YFP. All HCV fusions were expressed and localized to specific subcellular compartments, indicating that they were functional. FACS-FRET measurements identified a total of 20 interactions; 13 of these were previously described and have now been confirmed in living cells via our method. Among the seven novel protein binding pairs, HCV p7 plays a pivotal role. It binds to the HCV capsid protein Core and the two glycoproteins E1 and E2. These interplays were further demonstrated in the relevant context of Huh7.5 liver cells expressing infectious HCV. Our work demonstrates the feasibility of rapidly generating small interaction networks via FACS-FRET and defines the network of intra-HCV protein interactions. Furthermore, our data support an important role of p7 in HCV assembly.

Indexed as

Protein Interaction MapsCell LineFlow CytometryFluorescence Resonance Energy TransferHEK293 CellsHepacivirusHepatocytesHumansProtein BindingProteomeViral ProteinsVirus AssemblyProteomeViral Proteins

Identifiers

PMID24797426
PMCPMC4083108
OpenAlexW2103944196

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.