Newly synthesized dengue-2 virus nonstructural protein NS1 is a soluble protein but becomes partially hydrophobic and membrane-associated after dimerization.
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.
Winkler
G
G
Department of Molecular Genetics and Microbiology, Robert Wood Johnson Medical School, University of Medicine and Dentistry, Piscataway, New Jersey 08854-5635.
Maxwell
S E
SE
Ruemmler
C
C
Stollar
V
V
D000818:Animals; D002213:Capsid / Q000096:biosynthesis / Q000502:physiology*; D002460:Cell Line; D006224:Cricetinae; D003716:Dengue Virus / Q000648:ultrastructure*; D006023:Glycoproteins / Q000502:physiology; D006031:Glycosylation; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D012995:Solubility; D014758:Viral Core Proteins / Q000096:biosynthesis / Q000502:physiology*; D017361:Viral Nonstructural Proteins
D006023:Glycoproteins; D046911:Macromolecular Substances; D014758:Viral Core Proteins; D017361:Viral Nonstructural Proteins