Characterization of ATPase Activity of a Hepatitis C Virus NS3 Helicase Domain, and Analysis Involving Mercuric Reagents

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概要

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• The C-terminal two-thirds of nonstructural protein 3 (NS3) of hepatitis C virus (HCV) exhibits RNA-dependent NTPase/helicase activity. This enzyme is considered to be involved in viral replication and is expected to be one of the target molecules of antiHCV drugs. In a search for NTPase inhibitors specific to HCV, we expressed and purified the truncated NS3 NTPase/helicase domain. Here, we report the characterization of its RNA-dependent ATPase activity. This enzyme preferred Mg2+ and the optimal pH was 7.0. We further investigated the effects of heavy metal ions on the ATPase activity. The mercuric ion inhibited it significantly, the 50% inhibitory concentration being 49 nM. The fact that the inhibitory profile was competitive and that this inhibition was blocked in the presence of a large excess of cysteine or dithiothreitol, suggested that a cysteine residue in the DECH box was the main target site of mercury.

• 社団法人 日本生化学会の論文

著者

• Miyashiro Masahiko

  Discovery & Pharmacology Research Laboratories Tanabe Seiyaku Co. Ltd.

• Kyono Kiyoshi

  Medicinal Chemistry Research Laboratories Tanabe Seiyaku Co. Ltd.

• TAGUCHI Ikuhiko

  Discovery & Pharmacology Research Laboratories, Tanabe Seiyaku Co., Ltd.

関連論文

• Cloning and Characterization of Zymomonas mobilis Genes Encoding Extracellular Levansucrase and Invertase
• Expression and Purification of a Hepatitis C Virus NS3/4A Complex, and Characterization of Its Helicase Activity with the Scintillation Proximity Assay System
• Characterization of ATPase Activity of a Hepatitis C Virus NS3 Helicase Domain, and Analysis Involving Mercuric Reagents
• Characterization of ATPase Activity of a Hepatitis C Virus NS3 Helicase Domain, and Analysis Involving Mercuric Reagents

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