Abstract:
: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.
journal_name
Virologyjournal_title
Virologyauthors
Winkler G,Maxwell SE,Ruemmler C,Stollar Vdoi
10.1016/0042-6822(89)90544-8subject
Has Abstractpub_date
1989-07-01 00:00:00pages
302-5issue
1eissn
0042-6822issn
1096-0341journal_volume
171pub_type
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