scholarly journals Neutralization of Pseudotyped Vesicular Stomatitis Virus Expressing Hepatitis C Virus Envelope Glycoprotein 1 or 2 by Serum from Patients

2002 ◽  
Vol 185 (8) ◽  
pp. 1165-1169 ◽  
Author(s):  
L. Martin Lagging ◽  
Keith Meyer ◽  
Johan Westin ◽  
Rune Wejstål ◽  
Gunnar Norkrans ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Vesicular Stomatitis Virus ◽  
Envelope Glycoprotein ◽  
Virus Envelope ◽  
Vesicular Stomatitis

scholarly journals Replication-Competent Recombinant Vesicular Stomatitis Virus Encoding Hepatitis C Virus Envelope Proteins

2007 ◽  
Vol 81 (16) ◽  
pp. 8601-8612 ◽  
Author(s):  
Hideki Tani ◽  
Yasumasa Komoda ◽  
Eiko Matsuo ◽  
Kensuke Suzuki ◽  
Itsuki Hamamoto ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Cell Lines ◽  
Vesicular Stomatitis Virus ◽  
Envelope Proteins ◽  
Virus Envelope ◽  
Focus Formation ◽  
A Genome ◽  
Huh7 Cells ◽  
Vesicular Stomatitis

ABSTRACT Although in vitro replication of the hepatitis C virus (HCV) JFH1 clone of genotype 2a (HCVcc) has been developed, a robust cell culture system for the 1a and 1b genotypes, which are the most prevalent viruses in the world and resistant to interferon therapy, has not yet been established. As a surrogate virus system, pseudotype viruses transiently bearing HCV envelope proteins based on the vesicular stomatitis virus (VSV) and retrovirus have been developed. Here, we have developed a replication-competent recombinant VSV with a genome encoding unmodified HCV E1 and E2 proteins in place of the VSV envelope protein (HCVrv) in human cell lines. HCVrv and a pseudotype VSV bearing the unmodified HCV envelope proteins (HCVpv) generated in 293T or Huh7 cells exhibited high infectivity in Huh7 cells. Generation of infectious HCVrv was limited in some cell lines examined. Furthermore, HCVrv but not HCVpv was able to propagate and form foci in Huh7 cells. The infection of Huh7 cells with HCVpv and HCVrv was neutralized by anti-hCD81 and anti-E2 antibodies and by sera from chronic HCV patients. The infectivity of HCVrv was inhibited by an endoplasmic reticulum α-glucosidase inhibitor, N-(n-nonyl) deoxynojirimycin (Nn-DNJ), but not by a Golgi mannosidase inhibitor, deoxymannojirimycin. Focus formation of HCVrv in Huh7 cells was impaired by Nn-DNJ treatment. These results indicate that the HCVrv developed in this study can be used to study HCV envelope proteins with respect to not only the biological functions in the entry process but also their maturation step.

scholarly journals Probing the antigenicity of hepatitis C virus envelope glycoprotein complex by high-throughput mutagenesis

2017 ◽  
Vol 13 (12) ◽  
pp. e1006735 ◽  
Author(s):  
Radhika Gopal ◽  
Kelli Jackson ◽  
Netanel Tzarum ◽  
Leopold Kong ◽  
Andrew Ettenger ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Throughput ◽  
Envelope Glycoprotein ◽  
Virus Envelope ◽  
Glycoprotein Complex

scholarly journals Hepatitis C Virus Envelope Glycoprotein Fitness Defines Virus Population Composition following Transmission to a New Host

2012 ◽  
Vol 86 (22) ◽  
pp. 11956-11966 ◽  
Author(s):  
R. J. P. Brown ◽  
N. Hudson ◽  
G. Wilson ◽  
S. U. Rehman ◽  
S. Jabbari ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Virus Population ◽  
Population Composition ◽  
Virus Envelope ◽  
New Host

scholarly journals Immunogenicity and functional characterization of Leishmania-derived hepatitis C virus envelope glycoprotein complex

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Katarzyna Grzyb ◽  
Anna Czarnota ◽  
Agnieszka Brzozowska ◽  
Anna Cieślik ◽  
Łukasz Rąbalski ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Functional Characterization ◽  
Virus Envelope ◽  
Glycoprotein Complex

scholarly journals Identification of Amino Acid Residues in CD81 Critical for Interaction with Hepatitis C Virus Envelope Glycoprotein E2

2000 ◽  
Vol 74 (8) ◽  
pp. 3642-3649 ◽  
Author(s):  
Adrian Higginbottom ◽  
Elizabeth R. Quinn ◽  
Chiung-Chi Kuo ◽  
Mike Flint ◽  
Louise H. Wilson ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Amino Acid ◽  
Envelope Glycoprotein ◽  
Tertiary Structure ◽  
Antibody Binding ◽  
Viral Envelope ◽  
Amino Acid Residues ◽  
Virus Envelope ◽  
Glycoprotein E2

ABSTRACT Human CD81 has been previously identified as the putative receptor for the hepatitis C virus envelope glycoprotein E2. The large extracellular loop (LEL) of human CD81 differs in four amino acid residues from that of the African green monkey (AGM), which does not bind E2. We mutated each of the four positions in human CD81 to the corresponding AGM residues and expressed them as soluble fusion LEL proteins in bacteria or as complete membrane proteins in mammalian cells. We found human amino acid 186 to be critical for the interaction with the viral envelope glycoprotein. This residue was also important for binding of certain anti-CD81 monoclonal antibodies. Mutating residues 188 and 196 did not affect E2 or antibody binding. Interestingly, mutation of residue 163 increased both E2 and antibody binding, suggesting that this amino acid contributes to the tertiary structure of CD81 and its ligand-binding ability. These observations have implications for the design of soluble high-affinity molecules that could target the CD81-E2 interaction site(s).

1226 HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN SIGNATURES AND RESISTANCE TO ANTIVIRAL TREATMENT

2011 ◽  
Vol 54 ◽  
pp. S484
Author(s):  
R. Moenne-Loccoz ◽  
A. Velay ◽  
J. Murray ◽  
F. Habersetzer ◽  
M. Doffoël ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Antiviral Treatment ◽  
Virus Envelope

scholarly journals Structure of Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Site 412 to 423 in Complex with Antibody AP33

2012 ◽  
Vol 86 (23) ◽  
pp. 13085-13088 ◽  
Author(s):  
L. Kong ◽  
E. Giang ◽  
T. Nieusma ◽  
J. B. Robbins ◽  
M. C. Deller ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Antigenic Site ◽  
Virus Envelope ◽  
Glycoprotein E2
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