PMID: 11906735Mar 22, 2002Paper

Cloning and molecular characterization of human high affinity antibody fragments against Hepatitis C virus NS3 helicase

Journal of Virological Methods
Kathi TessmannT Heintges

Abstract

Hepatitis C Virus (HCV) non-structural protein 3 (NS3) helicase is essential for viral replication. Cloning of human antibody fragments for binding and inhibiting HCV helicase intracellularly (intracellular immunization) was attempted. A phage display system was employed to isolate human sFv fragments. A large phagemid library was cloned from patients infected with HCV. Phages expressing human sFv fragments with binding activity against NS3 were highly enriched during affinity selection. Selected sFv antibody fragments showed high affinity to HCV helicase. The variable domains of the cloned antibody fragments were sequenced and their germ-line origin was determined. K(D) values describing affinity of sFv to NS3 were measured by competition-EIA. Bacterially expressed recombinant human high affinity antibodies can be used for diagnostic and therapeutic purposes. Further experiments will select antibody fragments inhibiting NS3 helicase. Employing vectors for transduction of the encoding cDNA into infected cells might be a novel gene therapy strategy for intracellular immunization against chronic HCV infection.

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Citations

Mar 24, 2005·Journal of Molecular Biology·Meital Gal-TanamyItai Benhar
Nov 9, 2005·Microscopy Research and Technique·Srikanta DashRobert Garry
Aug 13, 2008·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Juliane KartheTobias Heintges
Aug 15, 2003·The Journal of General Virology·Olga ArtsaenkoTobias Heintges
Nov 13, 2003·Expert Opinion on Emerging Drugs·F Fred PoordadPaul Martin

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