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

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

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 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

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 A Point Mutation Leading to Hepatitis C Virus Escape from Neutralization by a Monoclonal Antibody to a Conserved Conformational Epitope

2008 ◽  
Vol 82 (12) ◽  
pp. 6067-6072 ◽  
Author(s):  
Zhen-Yong Keck ◽  
Oakley Olson ◽  
Meital Gal-Tanamy ◽  
Jinming Xia ◽  
Arvind H. Patel ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Vaccine Development ◽  
Human Monoclonal Antibody ◽  
Conformational Epitope ◽  
Single Amino Acid ◽  
Effective Vaccine ◽  
Linear Sequence ◽  
Virus Escape

ABSTRACT A challenge in hepatitis C virus (HCV) vaccine development is defining conserved protective epitopes. A cluster of these epitopes comprises an immunodominant domain on the E2 glycoprotein, designated domain B. CBH-2 is a neutralizing human monoclonal antibody to a domain B epitope that is highly conserved. Alanine scanning demonstrated that the epitope involves residues G523, G530, and D535 that are also contact residues for E2 binding to CD81, a coreceptor required for virus entry into cells. However, another residue, located at position 431 and thus at a considerable distance in the linear sequence of E2, also contributes to the CBH-2 epitope. A single amino acid substitution at this residue results in escape from CBH-2-mediated neutralization in a genotype 1a virus. These results highlight the challenges inherent in developing HCV vaccines and show that an effective vaccine must induce antibodies to both conserved and more invariant epitopes to minimize virus escape.

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 Monoclonal Antibody AP33 Defines a Broadly Neutralizing Epitope on the Hepatitis C Virus E2 Envelope Glycoprotein

2005 ◽  
Vol 79 (17) ◽  
pp. 11095-11104 ◽  
Author(s):  
Ania Owsianka ◽  
Alexander W. Tarr ◽  
Vicky S. Juttla ◽  
Dimitri Lavillette ◽  
Birke Bartosch ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Envelope Glycoprotein ◽  
Envelope Protein ◽  
Hypervariable Region ◽  
Neutralizing Antibody ◽  
Broadly Neutralizing Antibody ◽  
New Treatments ◽  
Potent Neutralization

ABSTRACT Hepatitis C virus (HCV) remains a significant threat to the general health of the world's population, and there is a pressing need for the development of new treatments and preventative vaccines. Here, we describe the generation of retrovirus-based pseudoparticles (HCVpp) incorporating a panel of full-length E1E2 clones representative of the major genotypes 1 through 6, and their application to assess the reactivity and neutralizing capability of antisera and monoclonal antibodies raised against portions of the HCV E2 envelope protein. Rabbit antisera raised against either the first hypervariable region or ectodomain of E2 showed limited and strain specific neutralization. By contrast, the monoclonal antibody (MAb) AP33 demonstrated potent neutralization of infectivity against HCVpp carrying E1E2 representative of all genotypes tested. The concentration of AP33 required to achieve 50% inhibition of infection by HCVpp of diverse genotypes ranged from 0.6 to 32 μg/ml. The epitope recognized by MAb AP33 is linear and highly conserved across different genotypes of HCV. Thus, identification of a broadly neutralizing antibody that recognizes a linear epitope is likely to be of significant benefit to future vaccine and therapeutic antibody development.

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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