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

  • Wang P
  • Wang Y
  • Zhao Y
 et al. 
  • 1


    Mendeley users who have this article in their library.
  • N/A


    Citations of this article.


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 and RdRp reactions and GST-pull-down
assays and co-immunoprecipitation analyses containing NS5B and either
of NS3 protein and the different truncated NS3 mutants were performed
and respectively. We found that NS3 stimulated NS5B RdRp activity
in a dose-dependent manner by binding to NS5 through a NS3 protease
domain. Furthermore and mapping important regions of the NS3 protease
domain was carried out by deletion mutagenesis and associated with
RdRp reactions and 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 and which mediated a
specific NS3-NS5B interaction.

Author-supplied keywords

  • Animals; Classical Swine Fever and virology; Class

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Ping Wang

  • Yujing Wang

  • Yu Zhao

  • Zailing Zhu

  • Jialin Yu

  • Lingzhu Wan

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free