ArticleVirology2014
The NS5A-binding heat shock proteins HSC70 and HSP70 play distinct roles in the hepatitis C viral life cycle.
Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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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.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Comparative IP-MS Reveals HSPA5 and HSPA8 Interacting with Hemagglutinin Protein to Promote the Replication of Influenza A Virus.Pathogens (Basel, Switzerland) · 2025Article
- HSP70 positively regulates translation by interacting with the IRES and stabilizes the viral structural proteins VP1 and VP3 to facilitate duck hepatitis A virus type 1 replication.Veterinary research · 2024Article
- New Insights into the Role and Therapeutic Potential of Heat Shock Protein 70 in Bovine Viral Diarrhea Virus Infection.Microorganisms · 2023Review
- Network pharmacology and experimental validation to reveal the target of matrine against PRRSV.iScience · 2023Article
- The relationship between protein modified folding molecular network and Alzheimer's disease pathogenesis based on BAG2-HSC70-STUB1-MAPT expression patterns analysis.Frontiers in aging neuroscience · 2023Article
- Host cell stress response as a predictor of COVID-19 infectivity and disease progression.Frontiers in molecular biosciences · 2022Review
- Pathogenesis and virulence of flavivirus infections.Virulence · 2021Review
- Heat shock protein 70 could enhance porcine epidemic diarrhoea virus replication by interacting with membrane proteins.Veterinary research · 2021Article
- Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021Review
- Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code.The Journal of biological chemistry · 2020Review
- Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.Signal transduction and targeted therapy · 2020Review
- Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay.Cold Spring Harbor perspectives in biology · 2020Review
- Hepatitis C Virus NS5A Protein Promotes the Lysosomal Degradation of Hepatocyte Nuclear Factor 1α via Chaperone-Mediated Autophagy.Journal of virology · 2018Article
- Rewiring cellular networks by members of the Flaviviridae family.Nature reviews. Microbiology · 2018Review
- Halogenated Chrysins Inhibit Dengue and Zika Virus Infectivity.Scientific reports · 2017Article
- Article
- Allosteric heat shock protein 70 inhibitors block hepatitis C virus assembly.International journal of antimicrobial agents · 2016Article
- Identification of Viral and Host Proteins That Interact with Murine Gammaherpesvirus 68 Latency-Associated Nuclear Antigen during Lytic Replication: a Role for Hsc70 in Viral Replication.Journal of virology · 2016Article
- Chaperones in hepatitis C virus infection.World journal of hepatology · 2016Review
- Activation of Tomato Bushy Stunt Virus RNA-Dependent RNA Polymerase by Cellular Heat Shock Protein 70 Is Enhanced by Phospholipids In Vitro.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
We previously identified HSP70 and HSC70 in complex with NS5A in a proteomic screen. Here, coimmunoprecipitation studies confirmed NS5A/HSC70 complex formation during infection, and immunofluorescence studies showed NS5A and HSC70 to colocalize. Unlike HSP70, HSC70 knockdown did not decrease viral protein levels. Rather, intracellular infectious virion assembly was significantly impaired by HSC70 knockdown. We also discovered that both HSC70 nucleotide binding and substrate binding domains directly bind NS5A whereas only the HSP70 nucleotide binding domain does. Knockdown of both HSC70 and HSP70 demonstrated an additive reduction in virus production. This data suggests that HSC70 and HSP70 play discrete roles in the viral life cycle. Investigation of these different functions may facilitate developing of novel strategies that target host proteins to treat HCV infection.
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Registered trials
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.