Structure and function of the Zika virus full-length NS5 protein

Baoyu Zhao, Guanghui Yi, Fenglei Du, Yin-Chih Chuang, Robert C. Vaughan, Banumathi Sankaran, C. Cheng Kao () and Pingwei Li ()
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Baoyu Zhao: Texas A&M University
Guanghui Yi: Indiana University
Fenglei Du: Texas A&M University
Yin-Chih Chuang: Indiana University
Robert C. Vaughan: Indiana University
Banumathi Sankaran: Molecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology
C. Cheng Kao: Indiana University
Pingwei Li: Texas A&M University

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract The recent outbreak of Zika virus (ZIKV) has infected over 1 million people in over 30 countries. ZIKV replicates its RNA genome using virally encoded replication proteins. Nonstructural protein 5 (NS5) contains a methyltransferase for RNA capping and a polymerase for viral RNA synthesis. Here we report the crystal structures of full-length NS5 and its polymerase domain at 3.0 Å resolution. The NS5 structure has striking similarities to the NS5 protein of the related Japanese encephalitis virus. The methyltransferase contains in-line pockets for substrate binding and the active site. Key residues in the polymerase are located in similar positions to those of the initiation complex for the hepatitis C virus polymerase. The polymerase conformation is affected by the methyltransferase, which enables a more efficiently elongation of RNA synthesis in vitro. Overall, our results will contribute to future studies on ZIKV infection and the development of inhibitors of ZIKV replication.

Date: 2017
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DOI: 10.1038/ncomms14762

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