Definition of a conserved immunodominant domain on hepatitis C virus E2 glycoprotein by neutralizing human monoclonal antibodies

Zhen Yong Keck; Ta Kai Li; Jinming Xia; Meital Gal-Tanamy; Oakley Olson; Sophia H. Li; Arvind H. Patel; Jonathan K. Ball; Stanley M. Lemon; Steven K.H. Foung

doi:10.1128/JVI.02475-07

Definition of a conserved immunodominant domain on hepatitis C virus E2 glycoprotein by neutralizing human monoclonal antibodies

Zhen Yong Keck, Ta Kai Li, Jinming Xia, Meital Gal-Tanamy, Oakley Olson, Sophia H. Li, Arvind H. Patel, Jonathan K. Ball, Stanley M. Lemon, Steven K.H. Foung

Research output: Contribution to journal › Article › peer-review

107 Scopus citations

Abstract

Development of a successful hepatitis C virus (HCV) vaccine requires the definition of neutralization epitopes that are conserved among different HCV genotypes. Five human monoclonal antibodies (HMAbs) are described that cross-compete with other antibodies to a cluster of overlapping epitopes, previously designated domain B. Each HMAb broadly neutralizes retroviral pseudotype particles expressing HCV E1 and E2 glycoproteins, as well as the infectious chimeric genotype 1a and genotype 2a viruses. Alanine substitutions of residues within a region of E2 involved in binding to CD81 showed that critical E2 contact residues involved in the binding of representative antibodies are identical to those involved in the binding of E2 to CD81.

Original language	English
Pages (from-to)	6061-6066
Number of pages	6
Journal	Journal of Virology
Volume	82
Issue number	12
DOIs	https://doi.org/10.1128/JVI.02475-07
State	Published - Jun 2008
Externally published	Yes

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abstract = "Development of a successful hepatitis C virus (HCV) vaccine requires the definition of neutralization epitopes that are conserved among different HCV genotypes. Five human monoclonal antibodies (HMAbs) are described that cross-compete with other antibodies to a cluster of overlapping epitopes, previously designated domain B. Each HMAb broadly neutralizes retroviral pseudotype particles expressing HCV E1 and E2 glycoproteins, as well as the infectious chimeric genotype 1a and genotype 2a viruses. Alanine substitutions of residues within a region of E2 involved in binding to CD81 showed that critical E2 contact residues involved in the binding of representative antibodies are identical to those involved in the binding of E2 to CD81.",

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AU - Keck, Zhen Yong

AU - Li, Ta Kai

AU - Xia, Jinming

AU - Gal-Tanamy, Meital

AU - Olson, Oakley

AU - Li, Sophia H.

AU - Patel, Arvind H.

AU - Ball, Jonathan K.

AU - Lemon, Stanley M.

AU - Foung, Steven K.H.

PY - 2008/6

Y1 - 2008/6

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AB - Development of a successful hepatitis C virus (HCV) vaccine requires the definition of neutralization epitopes that are conserved among different HCV genotypes. Five human monoclonal antibodies (HMAbs) are described that cross-compete with other antibodies to a cluster of overlapping epitopes, previously designated domain B. Each HMAb broadly neutralizes retroviral pseudotype particles expressing HCV E1 and E2 glycoproteins, as well as the infectious chimeric genotype 1a and genotype 2a viruses. Alanine substitutions of residues within a region of E2 involved in binding to CD81 showed that critical E2 contact residues involved in the binding of representative antibodies are identical to those involved in the binding of E2 to CD81.

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Definition of a conserved immunodominant domain on hepatitis C virus E2 glycoprotein by neutralizing human monoclonal antibodies

Abstract

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