Extended surface for membrane association in Zika virus NS1 structure

Nat Struct Mol Biol. 2016 Sep;23(9):865-7. doi: 10.1038/nsmb.3268. Epub 2016 Jul 25.


The Zika virus, which has been implicated in an increase in neonatal microcephaly and Guillain-Barré syndrome, has spread rapidly through tropical regions of the world. The virulence protein NS1 functions in genome replication and host immune-system modulation. Here, we report the crystal structure of full-length Zika virus NS1, revealing an elongated hydrophobic surface for membrane association and a polar surface that varies substantially among flaviviruses.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Interaction Domains and Motifs
  • Protein Structure, Quaternary
  • Sf9 Cells
  • Spodoptera
  • Surface Properties
  • Viral Nonstructural Proteins / chemistry*
  • Virus Attachment
  • Zika Virus / ultrastructure


  • Viral Nonstructural Proteins