Newly synthesized dengue-2 virus nonstructural protein NS1 is a soluble protein but becomes partially hydrophobic and membrane-associated after dimerization

Virology. 1989 Jul;171(1):302-5. doi: 10.1016/0042-6822(89)90544-8.


In a previous paper (G. Winkler, V. B. Randolph, G. R. Cleaves, T. E. Ryan, and V. Stollar, 1988, Virology 162, 187-196) we showed that the newly synthesized dengue-2 virus nonstructural protein, NS1, exists briefly as a monomer and then undergoes dimerization. We demonstrate here that the dimerization of NS1 is associated with a change in hydrophobicity and sedimentability of this protein. Newly synthesized monomeric NS1 is a hydrophilic and water-soluble protein which cannot be pelleted at 75,000 g. After dimerization, however, NS1 showed increased hydrophobicity in a Triton X-114 phase partitioning system and was completely pelletable at 75,000 g; these findings are consistent with NS1 becoming membrane-associated. In experiments in which infected cells were treated with tunicamycin it was shown that the glycosylation of NS1 was not required for either the dimerization or the membrane association.

Publication types

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

MeSH terms

  • Animals
  • Capsid / biosynthesis
  • Capsid / physiology*
  • Cell Line
  • Cricetinae
  • Dengue Virus / ultrastructure*
  • Glycoproteins / physiology
  • Glycosylation
  • Macromolecular Substances
  • Molecular Weight
  • Protein Binding
  • Solubility
  • Viral Core Proteins / biosynthesis
  • Viral Core Proteins / physiology*
  • Viral Nonstructural Proteins


  • Glycoproteins
  • Macromolecular Substances
  • Viral Core Proteins
  • Viral Nonstructural Proteins