ArticleJournal of virology2002
Detection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKR.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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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Who cites it
36 citing papers in PubMed, 92 citations in OpenAlex.
- Human Viral Oncoproteins and Ubiquitin-Proteasome System.Global medical genetics · 2024Review
- Role of Immunological Cells in Hepatocellular Carcinoma Disease and Associated Pathways.ACS pharmacology & translational science · 2023Review
- Hepatitis C Virus Nonstructural Protein 5A Interacts with Immunomodulatory Kinase IKKε to Negatively Regulate Innate Antiviral Immunity.Molecules and cells · 2022Article
- Protein kinase R is an innate immune sensor of proteotoxic stress via accumulation of cytoplasmic IL-24.Science immunology · 2022Article
- Coevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.Scientific reports · 2016Article
- Chaperones in hepatitis C virus infection.World journal of hepatology · 2016Review
- Hepatitis C virus comes for dinner: How the hepatitis C virus interferes with autophagy.World journal of gastroenterology · 2015Review
- Proteasome- and ethanol-dependent regulation of HCV-infection pathogenesis.Biomolecules · 2014Review
- The role of chemokines in hepatitis C virus-mediated liver disease.International journal of molecular sciences · 2014Review
- Protein kinase expression as a predictive factor for interferon response in chronic hepatitis C patients.Journal of advanced research · 2014Article
- Article
- Unfolded protein response in hepatitis C virus infection.Frontiers in microbiology · 2014Review
- An insight into the diagnosis and pathogenesis of hepatitis C virus infection.World journal of gastroenterology · 2013Review
- Innate immune responses in hepatitis C virus infection.Seminars in immunopathology · 2013Review
- Hepatitis C Virus Envelope Protein E1 Binds PERK and Represses the Unfolded Protein Response.The open virology journal · 2013Article
- dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection.Viruses · 2012Review
- Roles of the two distinct proteasome pathways in hepatitis C virus infection.World journal of virology · 2012Article
- Article
- Zinc mesoporphyrin induces rapid proteasomal degradation of hepatitis C nonstructural 5A protein in human hepatoma cells.Gastroenterology · 2010Article
- Bax inhibitor-1 down-regulation in the progression of chronic liver diseases.BMC gastroenterology · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The hepatitis C virus (HCV) envelope protein E2 has been shown to accumulate in the lumen of the endoplasmic reticulum (ER) as a properly folded glycoprotein as well as large aggregates of misfolded proteins. In the present study, we have identified an additional unglycosylated species, with an apparent molecular mass of 38 kDa (E2-p38). In contrast to the glycosylated E2, E2-p38 is significantly less stable and is degraded through the proteasome pathway. Correspondingly, E2-p38 is found to be ubiquitinated. E2-p38 is localized mostly in the cytosol, in contrast to the glycosylated form, which is exclusively membrane associated. Alpha interferon (IFN-alpha) treatment or overexpression of the double-stranded RNA-activated protein kinase (PKR) significantly increased the stability of E2-p38, consistent with a previous report (D. R. Taylor, S. T. Shi, P. R. Romano, G. N. Barber, and M. M. Lai, Science 285:107-110, 1999) that E2 interacts with PKR and inhibits its kinase activity. Direct interaction between PKR and E2-p38, but not the glycosylated form of E2, was also observed. These results show that E2-p38 is the form of E2 that interacts with PKR in the cytosol and may contribute to the resistance of HCV to IFN-alpha. Thus, an ER protein can exist in the cytosol as an unglycosylated species and impair cellular functions.
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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.