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. © 2009 Humana Press, a part of Springer Science+Business Media, LLC.
CITATION STYLE
Frick, D. N., Ginzburg, O., & Lam, A. M. I. (2010). A method to simultaneously monitor hepatitis c virus NS3 helicase and protease activities. Methods in Molecular Biology, 587, 223–233. https://doi.org/10.1007/978-1-60327-355-8_16
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