Classical swine fever virus NS3 enhances RNA-dependent RNA polymerase activity by binding to NS5B

  • Wang P
  • Wang Y
  • Zhao Y
 et al. 
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Abstract

NS3 of pestiviruses contains a protease domain and a RNA helicase/NTPase domain. Contradictory results have been reported regarding NS3 in RNA synthesis. To investigate the effect of NS3 on classical swine fever virus (CSFV) NS5B RNA-dependent RNA polymerase activity (RdRp) activity and NS3-NS5B interaction, RdRp reactions, GST-pull-down assays and co-immunoprecipitation analyses containing NS5B and either of NS3 protein and the different truncated NS3 mutants were performed, respectively. We found that NS3 stimulated NS5B RdRp activity in a dose-dependent manner by binding to NS5 through a NS3 protease domain. Furthermore, mapping important regions of the NS3 protease domain was carried out by deletion mutagenesis, associated with RdRp reactions, GST-pull-down assays and co-immunoprecipitation analyses. Results showed that stimulation of CSFV NS5B RdRp activity was obtained by NS3 binding to NS5B through a 31-amino acid fragment at the N-terminal end of NS3 protease domain, which mediated a specific NS3-NS5B interaction. © 2009 Elsevier B.V. All rights reserved.

Author-supplied keywords

  • Classical swine fever virus
  • NS3
  • NS3-NS5B interaction
  • NS5B

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Authors

  • Ping Wang

  • Yujing Wang

  • Yu Zhao

  • Zailing Zhu

  • Jialin Yu

  • Lingzhu Wan

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