Structure and function of the Zika virus full-length NS5 protein | Academic Article individual record
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.

authors
author list (cited authors)
Zhao, B., Yi, G., Du, F., Chuang, Y., Vaughan, R. C., Sankaran, B., Kao, C. C., & Li, P.
publication date
2017
published in
keywords
  • RNA Replicase
  • Zika Virus
  • Methyltransferases
  • Rna Caps
  • Viral Nonstructural Proteins
  • Substrate Specificity
  • Protein Conformation
  • Virus Replication
  • Crystallography, X-Ray
altmetric score

112.35

citation count

88