scholarly journals Topological changes in the transmembrane domains of hepatitis C virus envelope glycoproteins

2002 ◽  
Vol 21 (12) ◽  
pp. 2893-2902 ◽  
Author(s):  
L. Cocquerel
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transmembrane Domains ◽  
Envelope Glycoproteins ◽  
Virus Envelope ◽  
Topological Changes

scholarly journals The Transmembrane Domains of Hepatitis C Virus Envelope Glycoproteins E1 and E2 Play a Major Role in Heterodimerization

2000 ◽  
Vol 275 (40) ◽  
pp. 31428-31437 ◽  
Author(s):  
Anne Op De Beeck ◽  
Roland Montserret ◽  
Sandrine Duvet ◽  
Laurence Cocquerel ◽  
René Cacan ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transmembrane Domains ◽  
Envelope Glycoproteins ◽  
Virus Envelope

Hepatitis C virus envelope glycoproteins complementation patterns and the role of the ecto- and transmembrane domains

2009 ◽  
Vol 385 (2) ◽  
pp. 257-262 ◽  
Author(s):  
Xiaojing Lin ◽  
Yonghui Zhang ◽  
Shengli Bi ◽  
Jian Lu ◽  
Honglan Zhao ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Transmembrane Domains ◽  
Envelope Glycoproteins ◽  
Virus Envelope

330 MOLECULAR SIGNATURES OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEINS AND RESPONSE TO ANTIVIRAL TREATMENT

2009 ◽  
Vol 50 ◽  
pp. S128
Author(s):  
R. Moenne-Loccoz ◽  
C. Rajafinjatovo ◽  
S. Fafi-Kremer ◽  
F. Habersetzer ◽  
A. Ananna ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Antiviral Treatment ◽  
Envelope Glycoproteins ◽  
Molecular Signatures ◽  
Virus Envelope

Mapping and characterization of B cell linear epitopes in the conservative regions of hepatitis C virus envelope glycoproteins

2002 ◽  
Vol 9 (3) ◽  
pp. 174-182 ◽  
Author(s):  
L. V. Olenina ◽  
L. I. Nikolaeva ◽  
B. N. Sobolev ◽  
N. P. Blokhina ◽  
A. I. Archakov ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
B Cell ◽  
Envelope Glycoproteins ◽  
Virus Envelope ◽  
Linear Epitopes

scholarly journals Hepatitis C Virus Envelope Glycoproteins: A Balancing Act of Order and Disorder

2018 ◽  
Vol 9 ◽  
Author(s):  
Samantha A. Yost ◽  
Yuanyuan Wang ◽  
Joseph Marcotrigiano
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoproteins ◽  
Virus Envelope ◽  
Order And Disorder

B-Cell Linear Epitopes in the Conservative Regions of Hepatitis C Virus Envelope Glycoproteins

2001 ◽  
pp. 1031-1032
Author(s):  
Ekaterina F. Kolesanova ◽  
Ludmila V. Olenina ◽  
Boris N. Sobolev ◽  
Ludmila I. Nikolaeva ◽  
Alexander I. Archakov
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
B Cell ◽  
Envelope Glycoproteins ◽  
Virus Envelope ◽  
Linear Epitopes

scholarly journals Characterization of Antibodies Induced by Vaccination with Hepatitis C Virus Envelope Glycoproteins

2010 ◽  
Vol 202 (6) ◽  
pp. 862-866 ◽  
Author(s):  
Ranjit Ray ◽  
Keith Meyer ◽  
Arup Banerjee ◽  
Arnab Basu ◽  
Stephen Coates ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoproteins ◽  
Virus Envelope

scholarly journals Transmembrane Domains of Hepatitis C Virus Envelope Glycoproteins: Residues Involved in E1E2 Heterodimerization and Involvement of These Domains in Virus Entry

2006 ◽  
Vol 81 (5) ◽  
pp. 2372-2381 ◽  
Author(s):  
Yann Ciczora ◽  
Nathalie Callens ◽  
François Penin ◽  
Eve-Isabelle Pécheur ◽  
Jean Dubuisson
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Mutational Analysis ◽  
Virus Entry ◽  
Envelope Glycoproteins ◽  
Insertion Mutagenesis ◽  
Virus Envelope ◽  
Central Regions ◽  
Tm Domain

ABSTRACT The transmembrane (TM) domains of hepatitis C virus (HCV) envelope glycoproteins E1 and E2 have been shown to play multiple roles during the biogenesis of the E1E2 heterodimer. By using alanine scanning insertion mutagenesis within the TM domains of HCV envelope glycoproteins, we have previously shown that the central regions of these domains as well as the N-terminal part of the TM domain of E1 are involved in heterodimerization. Here, we used a tryptophan replacement scan of these regions to identify individual residues that participate in those interactions. Our mutagenesis study identified at least four residues involved in heterodimerization: Gly 354, Gly 358, Lys 370, and Asp 728. Interestingly, Gly 354 and Gly 358 belong to a GXXXG oligomerization motif. Our tryptophan mutants were also used to generate retrovirus-based, HCV-pseudotyped particles (HCVpp) in order to analyze the effects of these mutations on virus entry. Surprisingly, two mutants consistently displayed higher infectivity compared to that of the wild type. In contrast, HCVpp infectivity was strongly affected for many mutants, despite normal E1E2 heterodimerization and normal levels of incorporation of HCV glycoproteins into HCVpp. The characterization of some of these HCVpp mutants in the recently developed in vitro fusion assay using fluorescent-labeled liposomes indicated that mutations reducing HCVpp infectivity without altering E1E2 heterodimerization affected the fusion properties of HCV envelope glycoproteins. In conclusion, this mutational analysis identified residues involved in E1E2 heterodimerization and revealed that the TM domains of HCV envelope glycoproteins play a major role in the fusion properties of these proteins.

New neutralizing antibody epitopes in hepatitis C virus envelope glycoproteins are revealed by dissecting peptide recognition profiles

Vaccine ◽  
2011 ◽  
Vol 30 (1) ◽  
pp. 69-77 ◽  
Author(s):  
Alla Kachko ◽  
Galina Kochneva ◽  
Galina Sivolobova ◽  
Antonina Grazhdantseva ◽  
Tatyana Lupan ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Neutralizing Antibody ◽  
Envelope Glycoproteins ◽  
Virus Envelope ◽  
Peptide Recognition ◽  
Antibody Epitopes

scholarly journals Role of N-Linked Glycans in the Functions of Hepatitis C Virus Envelope Proteins Incorporated into Infectious Virions

2010 ◽  
Vol 84 (22) ◽  
pp. 11905-11915 ◽  
Author(s):  
François Helle ◽  
Gabrielle Vieyres ◽  
Laure Elkrief ◽  
Costin-Ioan Popescu ◽  
Czeslaw Wychowski ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Neutralizing Antibodies ◽  
Point Mutations ◽  
Envelope Proteins ◽  
Envelope Glycoproteins ◽  
Virus Envelope ◽  
Humoral Immune ◽  
A Cell

ABSTRACT Hepatitis C virus (HCV) envelope glycoproteins are highly glycosylated, with generally 4 and 11 N-linked glycans on E1 and E2, respectively. Studies using mutated recombinant HCV envelope glycoproteins incorporated into retroviral pseudoparticles (HCVpp) suggest that some glycans play a role in protein folding, virus entry, and protection against neutralization. The development of a cell culture system producing infectious particles (HCVcc) in hepatoma cells provides an opportunity to characterize the role of these glycans in the context of authentic infectious virions. Here, we used HCVcc in which point mutations were engineered at N-linked glycosylation sites to determine the role of these glycans in the functions of HCV envelope proteins. The mutants were characterized for their effects on virus replication and envelope protein expression as well as on viral particle secretion, infectivity, and sensitivity to neutralizing antibodies. Our results indicate that several glycans play an important role in HCVcc assembly and/or infectivity. Furthermore, our data demonstrate that at least five glycans on E2 (denoted E2N1, E2N2, E2N4, E2N6, and E2N11) strongly reduce the sensitivity of HCVcc to antibody neutralization, with four of them surrounding the CD81 binding site. Altogether, these data indicate that the glycans associated with HCV envelope glycoproteins play roles at different steps of the viral life cycle. They also highlight differences in the effects of glycosylation mutations between the HCVpp and HCVcc systems. Furthermore, these carbohydrates form a “glycan shield” at the surface of the virion, which contributes to the evasion of HCV from the humoral immune response.

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