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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Baoyu Zhao & Guanghui Yi & Fenglei Du & Yin-Chih Chuang & Robert C. Vaughan & Banumathi Sankaran & C. Cheng Kao & Pingwei Li, 2017. "Structure and function of the Zika virus full-length NS5 protein," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14762
    DOI: 10.1038/ncomms14762
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