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 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

Characterization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia viruses.

1993 ◽  
Vol 67 (11) ◽  
pp. 6753-6761 ◽  
Author(s):  
R Ralston ◽  
K Thudium ◽  
K Berger ◽  
C Kuo ◽  
B Gervase ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Virus Envelope ◽  
Recombinant Vaccinia ◽  
Vaccinia Viruses

scholarly journals Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1

Virology ◽  
2018 ◽  
Vol 514 ◽  
pp. 30-41 ◽  
Author(s):  
Ahmed Atef Mesalam ◽  
Isabelle Desombere ◽  
Ali Farhoudi ◽  
Freya Van Houtte ◽  
Lieven Verhoye ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Human Monoclonal Antibody ◽  
Terminal Region ◽  
Virus Envelope ◽  
Antibody Targeting

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 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 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 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).

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