The RNA-dependent RNA polymerases of different members of the family Flaviviridae exhibit similar properties in vitro.

@article{Steffens1999TheRR,
  title={The RNA-dependent RNA polymerases of different members of the family Flaviviridae exhibit similar properties in vitro.},
  author={Silke Steffens and H. J. Thiel and Sven Erik Behrens},
  journal={The Journal of general virology},
  year={1999},
  volume={80 ( Pt 10)},
  pages={2583-90}
}
The virus-encoded RNA-dependent RNA polymerase (RdRp), which is required for replication of the positive-strand RNA genome, is a key enzyme of members of the virus family Flaviviridae. By using heterologously expressed proteins, we demonstrate that the 77 kDa NS5B protein of two pestiviruses, bovine viral diarrhoea virus and classical swine fever virus, and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro. As originally shown for the RdRp of hepatitis C virus… CONTINUE READING

5 Figures & Tables

Connections & Topics

Mentioned Connections BETA
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
As originally shown for the RdRp of hepatitis C virus , RNA synthesis catalysed by the pestivirus and flavivirus enzymes is strictly primer - dependent in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
As originally shown for the RdRp of hepatitis C virus , RNA synthesis catalysed by the pestivirus and flavivirus enzymes is strictly primer - dependent in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
By using heterologously expressed proteins , we demonstrate that the 77 kDa NS5B protein of two pestiviruses , bovine viral diarrhoea virus and classical swine fever virus , and the 100 kDa NS5 protein of the West Nile flavivirus possess RdRp activity in vitro .
All Topics