ArticleJournal of virology1999
The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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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
71 citing papers in PubMed, 151 citations in OpenAlex.
- Mapping Determinants of Hepatitis C Virus E1/E2 Transmembrane Interactions Using Intergenotypic Chimeras.Viruses · 2026Article
- Landscape of protein-protein interactions during hepatitis C virus assembly and release.Microbiology spectrum · 2024Article
- Structure of the hepatitis C virus E1E2 glycoprotein complex.Science (New York, N.Y.) · 2022Article
- The Molecular Basis for EViruses · 2021Article
- Hepatitis C virus E2 envelope glycoprotein produced in Nicotiana benthamiana triggers humoral response with virus-neutralizing activity in vaccinated mice.Plant biotechnology journal · 2021Article
- Characterization of Membrane Topology and Retention Signal of Pestiviral Glycoprotein E1.Journal of virology · 2021Article
- Interaction of Pestiviral E1 and E2 Sequences in Dimer Formation and Intracellular Retention.International journal of molecular sciences · 2021Article
- The EViruses · 2021Article
- Fusogenicity of the Ghana Virus (Viruses · 2019Article
- The unexpected structures of hepatitis C virus envelope proteins.Experimental and therapeutic medicine · 2017Article
- Hepatitis C Virus Is Released via a Noncanonical Secretory Route.Journal of virology · 2016Article
- Comparative Proteomics Reveals Important Viral-Host Interactions in HCV-Infected Human Liver Cells.PloS one · 2016Article
- The Replacement of 10 Non-Conserved Residues in the Core Protein of JFH-1 Hepatitis C Virus Improves Its Assembly and Secretion.PloS one · 2015Article
- Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Viruses · 2014Review
- Characterization of hepatitis C virus intra- and intergenotypic chimeras reveals a role of the glycoproteins in virus envelopment.Journal of virology · 2013Article
- The transmembrane domain of the adenovirus E3/19K protein acts as an endoplasmic reticulum retention signal and contributes to intracellular sequestration of major histocompatibility complex class I molecules.Journal of virology · 2013Article
- Interaction of hepatitis C virus core protein with janus kinase is required for efficient production of infectious viruses.Biomolecules & therapeutics · 2013Review
- The signal sequence of type II porcine reproductive and respiratory syndrome virus glycoprotein 3 is sufficient for endoplasmic reticulum retention.Journal of veterinary science · 2013Article
- Virion assembly and release.Current topics in microbiology and immunology · 2013Review
- A physical interaction between viral replicase and capsid protein is required for genome-packaging specificity in an RNA virus.Journal of virology · 2012Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis C virus (HCV) glycoproteins E1 and E2 assemble to form a noncovalent heterodimer which, in the cell, accumulates in the endoplasmic reticulum (ER). Contrary to what is observed for proteins with a KDEL or a KKXX ER-targeting signal, the ER localization of the HCV glycoprotein complex is due to a static retention in this compartment rather than to its retrieval from the cis-Golgi region. A static retention in the ER is also observed when E2 is expressed in the absence of E1 or for a chimeric protein containing the ectodomain of CD4 in fusion with the transmembrane domain (TMD) of E2. Although they do not exclude the presence of an intracellular localization signal in E1, these data do suggest that the TMD of E2 is an ER retention signal for HCV glycoprotein complex. In this study chimeric proteins containing the ectodomain of CD4 or CD8 fused to the C-terminal hydrophobic sequence of E1 were shown to be localized in the ER, indicating that the TMD of E1 is also a signal for ER localization. In addition, these chimeric proteins were not processed by Golgi enzymes, indicating that the TMD of E1 is responsible for true retention in the ER, without recycling through the Golgi apparatus. Together, these data suggest that at least two signals (TMDs of E1 and E2) are involved in ER retention of the HCV glycoprotein complex.
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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.