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

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 Role of N-Linked Glycans in the Functions of Hepatitis C Virus Envelope Glycoproteins

2005 ◽  
Vol 79 (13) ◽  
pp. 8400-8409 ◽  
Author(s):  
Anne Goffard ◽  
Nathalie Callens ◽  
Birke Bartosch ◽  
Czeslaw Wychowski ◽  
François-Loïc Cosset ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Glycosylation Site ◽  
Viral Envelope ◽  
Envelope Glycoproteins ◽  
Wild Type ◽  
Virus Envelope ◽  
Glycosylation Sites

ABSTRACT Hepatitis C virus (HCV) encodes two viral envelope glycoproteins. E1 contains 4 or 5 N-linked glycosylation sites and E2 contains up to 11, with most of the sites being well conserved, suggesting that they play an essential role in some functions of these proteins. For this study, we used retroviral pseudotyped particles harboring mutated HCV envelope glycoproteins to study these glycans. The mutants were named with an N followed by a number related to the relative position of the potential glycosylation site in each glycoprotein (E1N1 to E1N4 for E1 mutants and E2N1 to E2N11 for E2 mutants). The characterization of these mutants allowed us to define three phenotypes. For the first group (E1N3, E2N3, E2N5, E2N6, E2N7, and E2N9), the infectivities of the mutants were close to that of the wild type. The second group (E1N1, E1N2, E1N4, E2N1, and E2N11) contained mutants that were still infectious but whose infectivities were reduced to <50% that of the wild type. The third group (E2N2, E2N4, E2N8, and E2N10) contained mutants that had almost totally lost infectivity. The absence of infectivity of the E2N8 and E2N10 mutants was due to the lack of incorporation of the E1E2 heterodimer into HCVpp, which was due to misfolding of the heterodimer, as shown by immunoprecipitation with conformation-sensitive antibodies and by a CD81 pull-down assay. The absence of infectivity of the E2N2 and E2N4 mutants indicated that these two glycans are involved in controlling HCV entry. Altogether, the data indicate that some glycans of HCV envelope glycoproteins play a major role in protein folding and others play a role in HCV entry.

scholarly journals Characterization of Functional Hepatitis C Virus Envelope Glycoproteins

2004 ◽  
Vol 78 (6) ◽  
pp. 2994-3002 ◽  
Author(s):  
Anne Op De Beeck ◽  
Cécile Voisset ◽  
Birke Bartosch ◽  
Yann Ciczora ◽  
Laurence Cocquerel ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Conformational Changes ◽  
Structural Changes ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Envelope Glycoproteins ◽  
Functional Envelope

ABSTRACT Hepatitis C virus (HCV) encodes two envelope glycoproteins, E1 and E2, that assemble as a noncovalent heterodimer which is mainly retained in the endoplasmic reticulum. Because assembly into particles and secretion from the cell lead to structural changes in viral envelope proteins, characterization of the proteins associated with the virion is necessary in order to better understand how they mature to be functional in virus entry. There is currently no efficient and reliable cell culture system to amplify HCV, and the envelope glycoproteins associated with the virion have therefore not been characterized yet. Recently, infectious pseudotype particles that are assembled by displaying unmodified HCV envelope glycoproteins on retroviral core particles have been successfully generated. Because HCV pseudotype particles contain fully functional envelope glycoproteins, these envelope proteins, or at least a fraction of them, should be in a mature conformation similar to that on the native HCV particles. In this study, we used conformation-dependent monoclonal antibodies to characterize the envelope glycoproteins associated with HCV pseudotype particles. We showed that the functional unit is a noncovalent E1E2 heterodimer containing complex or hybrid type glycans. We did not observe any evidence of maturation by a cellular endoprotease during the transport of these envelope glycoproteins through the secretory pathway. These envelope glycoproteins were recognized by a panel of conformation-dependent monoclonal antibodies as well as by CD81, a molecule involved in HCV entry. The functional envelope glycoproteins associated with HCV pseudotype particles were also shown to be sensitive to low-pH treatment. Such conformational changes are likely necessary to initiate fusion.

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

scholarly journals Characterization of Hepatitis C Virus Interaction with Heparan Sulfate Proteoglycans

2015 ◽  
Vol 89 (7) ◽  
pp. 3846-3858 ◽  
Author(s):  
Yan Xu ◽  
Pierre Martinez ◽  
Karin Séron ◽  
Guangxiang Luo ◽  
Fabrice Allain ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Apolipoprotein E ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycans ◽  
Hcv Infection ◽  
Host Cells ◽  
Envelope Glycoproteins ◽  
Length Unit

ABSTRACTHepatitis C virus (HCV) entry involves binding to cell surface heparan sulfate (HS) structures. However, due to the lipoprotein-like structure of HCV, the exact contribution of virion components to this interaction remains controversial. Here, we investigated the relative contribution of HCV envelope proteins and apolipoprotein E in the HS-binding step. Deletion of hypervariable region 1, a region previously proposed to be involved in HS binding, did not alter HCV virion binding to HS, indicating that this region is not involved in this interaction in the context of a viral infection. Patient sera and monoclonal antibodies recognizing different regions of HCV envelope glycoproteins were also used in a pulldown assay with beads coated with heparin, a close HS structural homologue. Although isolated HCV envelope glycoproteins could interact with heparin, none of these antibodies was able to interfere with the virion-heparin interaction, strongly suggesting that at the virion surface, HCV envelope glycoproteins are not accessible for HS binding. In contrast, results from kinetic studies, heparin pulldown experiments, and inhibition experiments with anti-apolipoprotein E antibodies indicated that this apolipoprotein plays a major role in HCV-HS interaction. Finally, characterization of the HS structural determinants required for HCV infection by silencing of the enzymes involved in the HS biosynthesis pathway and by competition with modified heparin indicated thatN- and 6-O-sulfation but not 2-O-sulfation is required for HCV infection and that the minimum HS oligosaccharide length required for HCV infection is a decasaccharide. Together, these data indicate that HCV hijacks apolipoprotein E to initiate its interaction with specific HS structures.IMPORTANCEHepatitis C is a global health problem. Hepatitis C virus (HCV) infects approximately 130 million individuals worldwide, with the majority of cases remaining undiagnosed and untreated. In most infected individuals, the virus evades the immune system and establishes a chronic infection. As a consequence, hepatitis C is the leading cause of cirrhosis, end-stage liver disease, hepatocellular carcinoma, and liver transplantation. Virus infection is initiated by entry of the virus into the host cell. In this study, we provide new insights into the viral and cellular determinants involved in the first step of HCV entry, the binding of the virus to host cells. We show that apolipoprotein E is likely responsible for virus binding to heparan sulfate and thatN- and 6-O-sulfation of the heparan sulfate proteoglycans is required for HCV infection. In addition, the minimal HS length unit required for HCV infection is a decasaccharide.

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
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