Structure and function of the Zika virus full-length NS5 protein
Autor(es): Zhao, Baoyu; Yi, Guanghui; Du, Fenglei; Chuang, Yun-Chih; Vaughan, Robert C.; Sankaran, Banumathi; Kao, C. Cheng; Li, Pingwei
Resumo: 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
Palavras-Chave: Virus structures; X-ray crystallography
Imprenta: Nature Communications, n. 14762, 2017
Identificador do objeto digital: 10.1038/ncomms14762
Descritores: Zika virus - Proteins ; Zika virus - RNA ; ZIKA virus - Proteins ; ZIKA virus - RNA
Data de publicação: 2017
