Human monoclonal antibody to hepatitis C virus E1 glycoprotein that blocks virus attachment and viral infectivity

Zhen Yong Keck, Vicky M H Sung, Susan Perkins, Judy Rowe, Sudhir Paul, T. Jake Liang, Michael M C Lai, Steven K H Foung

Research output: Contribution to journalArticle

Abstract

Human antibodies elicited in response to hepatitis C virus (HCV) infection are anticipated to react with the native conformation of the viral envelope structure. Isolation of these antibodies as human monoclonal antibodies that block virus binding and entry will be useful in providing potential therapeutic reagents and for vaccine development. H-111, an antibody to HCV envelope 1 protein (E1) that maps to the YEVRNVSGVYH sequence and is located near the N terminus of E1 and is able to immunoprecipitate E1E2 heterodimers, is described. Binding of H-111 to HCV E1 genotypes 1a, 1b, 2b, and 3a indicates that the H-111 epitope is highly conserved. Sequence analysis of antibody V regions showed evidence of somatic and affinity maturation of H-111. Finally, H-111 blocks HCV-like particle binding to and HCV virion infection of target cells, suggesting the involvement of this epitope in virus binding and entry.

Original languageEnglish (US)
Pages (from-to)7257-7263
Number of pages7
JournalJournal of Virology
Volume78
Issue number13
DOIs
StatePublished - Jul 2004
Externally publishedYes

ASJC Scopus subject areas

  • Immunology

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  • Cite this

    Keck, Z. Y., Sung, V. M. H., Perkins, S., Rowe, J., Paul, S., Liang, T. J., Lai, M. M. C., & Foung, S. K. H. (2004). Human monoclonal antibody to hepatitis C virus E1 glycoprotein that blocks virus attachment and viral infectivity. Journal of Virology, 78(13), 7257-7263. https://doi.org/10.1128/JVI.78.13.7257-7263.2004