Journal
VIRUS RESEARCH
Volume 148, Issue 1-2, Pages 17-23Publisher
ELSEVIER
DOI: 10.1016/j.virusres.2009.11.015
Keywords
Classical swine fever virus; NS3; NS5B; NS3-NS5B interaction
Categories
Funding
- National Natural Science Foundation of China [30670445, 30870492]
- Shanghai Municipal Science and Technology Commission [07DZ12038, 08JC1416900]
- Shanghai Municipal Education Commission [08ZZ66]
- Shanghai Leading Academic Discipline Project [S30406]
- Leading Academic Discipline Project of Shanghai Normal University [DZL709]
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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. (c) 2009 Elsevier B.V. All rights reserved.
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