ArticleJournal of virology2000
Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 172 citations in OpenAlex.
- Landscape of protein-protein interactions during hepatitis C virus assembly and release.Microbiology spectrum · 2024Article
- Current Hepatitis C Vaccine Candidates Based on the Induction of Neutralizing Antibodies.Viruses · 2023Review
- HCV E1 influences the fitness landscape of E2 and may enhance escape from E2-specific antibodies.Virus evolution · 2023Article
- An Arginine-Rich Motif in the ORF2 capsid protein regulates the hepatitis E virus lifecycle and interactions with the host cell.PLoS pathogens · 2022Article
- Production and immunogenicity of different prophylactic vaccines for hepatitis C virus (Review).Experimental and therapeutic medicine · 2022Review
- Sites of vulnerability in HCV E1E2 identified by comprehensive functional screening.Cell reports · 2022Article
- Induction of broadly neutralizing antibodies using a secreted form of the hepatitis C virus E1E2 heterodimer as a vaccine candidate.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- 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
- From Structural Studies to HCV Vaccine Design.Viruses · 2021Review
- Design of a native-like secreted form of the hepatitis C virus E1E2 heterodimer.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Antigenic and immunogenic evaluation of permutations of soluble hepatitis C virus envelope protein E2 and E1 antigens.PloS one · 2021Article
- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
- Fluoxazolevir inhibits hepatitis C virus infection in humanized chimeric mice by blocking viral membrane fusion.Nature microbiology · 2020Article
- Modeling of the adsorption of a protein-fragment on kaolinite with potential antiviral activity.Applied clay science · 2020Article
- Functional Study of the C-Terminal Part of the Hepatitis C Virus E1 Ectodomain.Journal of virology · 2018Article
- Activity of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in sera of patients with hepatitis C.Archives of medical science : AMS · 2018Article
- A protein coevolution method uncovers critical features of the Hepatitis C Virus fusion mechanism.PLoS pathogens · 2018Article
- Role of Hepatitis C Virus Envelope Glycoprotein E1 in Virus Entry and Assembly.Frontiers in immunology · 2018Review
- The unexpected structures of hepatitis C virus envelope proteins.Experimental and therapeutic medicine · 2017Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For most membrane proteins, the transmembrane domain (TMD) is more than just an anchor to the membrane. The TMDs of hepatitis C virus (HCV) envelope proteins E1 and E2 are extreme examples of the multifunctionality of such membrane-spanning sequences. Indeed, they possess a signal sequence function in their C-terminal half, play a major role in endoplasmic reticulum localization of E1 and E2, and are potentially involved in the assembly of these envelope proteins. These multiple functions are supposed to be essential for the formation of the viral envelope. As for the other viruses of the family Flaviviridae, these anchor domains are composed of two stretches of hydrophobic residues separated by a short segment containing at least one fully conserved charged residue. Replacement of these charged residues by an alanine in HCV envelope proteins led to an alteration of all of the functions performed by their TMDs, indicating that these functions are tightly linked together. These data suggest that the charged residues of the TMDs of HCV glycoproteins play a key role in the formation of the viral envelope.
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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.