Structure and function of the Zika virus full-length NS5 protein. Academic Article uri icon

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 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.

published proceedings

  • Nat Commun

altmetric score

  • 109.6

author list (cited authors)

  • Zhao, B., Yi, G., Du, F., Chuang, Y., Vaughan, R. C., Sankaran, B., Kao, C. C., & Li, P.

citation count

  • 116

complete list of authors

  • Zhao, Baoyu||Yi, Guanghui||Du, Fenglei||Chuang, Yin-Chih||Vaughan, Robert C||Sankaran, Banumathi||Kao, C Cheng||Li, Pingwei

publication date

  • March 2017