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The RNA-Unwinding Activity of Hepatitis C Virus Non-Structural Protein 3 (NS3) Is Positively Modulated by Its Protease Domain

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Abstract:

The nonstructural protein 3 (NS3) of hepatitis C virus contains a protease domain at its amino terminus and RNA helicase domain at its carboxyl terminus. To identify optimal NS3 protein for developing screening assays, we expressed full-length NS3 protease/helicase and helicase domains from both HCV type 1a (H77 strain) and 1b (Con1 strain), using either E. coli or baculovirus expression systems. Our studies showed that the full-length NS3 proteins, either with or without the presence of the NS4A domain, from either strains were at least 10-fold more efficient than the corresponding helicase domains in unwinding partial duplex RNA substrates. These findings provide a rationale for the use of full-length NS3 in high throughput screening assays to identify potent small molecule inhibitors of this important target of HCV.

Keywords: baculovirus; coli; hcv; helicase domain; ns; protease domain; unwinding activity

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866053765716

Affiliations: GEPB, Mail code UE 0433, GlaxoSmithKline, 709 Swedeland Road, King of Prussia, PA 19406, USA.

Publication date: May 1, 2005

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2005/00000012/00000004/art00003
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