Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase

文献类型： 外文期刊

第一作者： Wen, Guoyuan

作者： Wen, Guoyuan;Xue, Jinnuo;Shen, Yanping;Zhang, Chuyu;Pan, Zishu;Wen, Guoyuan

作者机构：

关键词： Classical swine fever virus (CSFV);NS3;Helicase;NTPase;NS5B

期刊名称：VIRUS RESEARCH （ 影响因子：3.303； 五年影响因子：3.445 ）

ISSN： 0168-1702

年卷期： 2009 年 141 卷 1 期

页码：

收录情况： SCI

摘要： Classical swine fever virus (CSFV) nonstructural protein 3 (NS3) is believed to possess three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. In this report, we expressed NS3 helicase domain (NS3h) in E. coli and characterized its helicase activity. The NS3h helicase activity was dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn(2+), and required the substrates possessing a 3' un-base-paired region on the RNA template strand. The NS3h helicase activity was proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of the RNA substrates. We also investigated the modulation of NS3 NTPase/helicase activities by NS3 protease domain and NS5B, an RNA-dependent RNA polymerase (RdRp). Our data showed that the NS3 protease domain enhanced the helicase activity of NS3 but had no effect on its NTPase activity. For the truncated NS3 (helicase domain, NS3h), both NTPase and helicase activities were up-regulated by NS5B. However, for the full-length NS3 (NS3FL), the NTPase activity, but not the helicase activity, was stimulated by NS5B. Maltose-binding protein (MBP) pull-down as well as enzyme-linked immunosorbent assays confirmed the specific interaction between NS3 and NS5B. (C) 2009 Elsevier B.V. All rights reserved.

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