The structure of Zika virus NS5 reveals a conserved domain conformation

Boxiao Wang, Xiao-Feng Tan, Stephanie Thurmond, Zhi-Min Zhang, Asher Lin, Rong Hai () and Jikui Song ()
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Boxiao Wang: University of California, Riverside
Xiao-Feng Tan: University of California, Riverside
Stephanie Thurmond: University of California, Riverside
Zhi-Min Zhang: University of California, Riverside
Asher Lin: University of California, Riverside
Rong Hai: University of California, Riverside
Jikui Song: University of California, Riverside

Nature Communications, 2017, vol. 8, issue 1, 1-6

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms14763

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