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The structure of Zika virus NS5 reveals a conserved domain conformation.

  • Author(s): Wang, Boxiao
  • Tan, Xiao-Feng
  • Thurmond, Stephanie
  • Zhang, Zhi-Min
  • Lin, Asher
  • Hai, Rong
  • Song, Jikui
  • et al.
Abstract

The recent outbreak of Zika virus (ZIKV) has imposed a serious threat to public health. Here we report the crystal structure of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltransferase (MTase) and RNA-dependent RNA polymerase (RdRp) domains stack into one of the two alternative conformations of flavivirus NS5 proteins. The activity of this NS5 protein is verified through a de novo RdRp assay on a subgenomic ZIKV RNA template. Importantly, our structural analysis leads to the identification of a potential drug-binding site of ZIKV NS5, which might facilitate the development of novel antivirals for ZIKV.

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