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Updated: May 8, 2026
Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors
Published on: July 16, 2012
Structural and functional characterization of the single-chain Fv fragment from a unique HCV E1E2-specific monoclonal
Catherine Fallecker1, Nicolas Tarbouriech, Mohammed Habib
1Univ. Grenoble Alpes, Unit for Virus Host-Cell Interactions, F-38000 Grenoble, France; CNRS, Unit for Virus Host-Cell Interactions, F-38000 Grenoble, France; Unit for Virus Host-Cell Interactions, Univ. Grenoble Alpes-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble, France.
Abstract:
The nucleotide sequence of the unique neutralizing monoclonal antibody D32.10 raised against a conserved conformational epitope shared between E1 and E2 on the serum-derived hepatitis C virus (HCV) envelope was determined. Subsequently, the recombinant single-chain Fv fragment (scFv) was cloned and expressed in Escherichia coli, and its molecular characterization was assessed using multi-angle laser light scattering. The scFv mimicked the antibody in binding to the native serum-derived HCV particles from patients, as well as to envelope E1E2 complexes and E1, E2 glycoproteins carrying the viral epitope. The scFv D32.10 competed with the parental IgG for binding to antigen, and therefore could be a promising candidate for therapeutics and diagnostics.
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