Abstract
The hepatitis C virus NS3 protein contains an N-terminal serine protease and a C-terminal helicase that unwinds RNA or DNA duplexes. The HCV NS3 protein is the target for several antiviral drugs in clinical trials, which inhibit the protease function. A method is reported to simultaneously monitor the helicase and protease function of the NS3 protein in a single reaction using fluorescence spectroscopy and a single chain recombinant protein where NS3 is fused to its protease activator NS4A. The method monitors both activities together in real time and is amenable to high-throughput screening. This new procedure could be used to identify compounds that inhibit both the helicase and protease activity of NS3.
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Acknowledgments
This study was supported by a grant from the National Institutes of Health (AI052395).
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© 2009 Humana Press, a part of Springer Science+Business Media, LLC
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Frick, D.N., Ginzburg, O., Lam, A.M. (2009). A Method to Simultaneously Monitor Hepatitis C Virus NS3 Helicase and Protease Activities. In: Abdelhaleem, M. (eds) Helicases. Methods in Molecular Biology, vol 587. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60327-355-8_16
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DOI: https://doi.org/10.1007/978-1-60327-355-8_16
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