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Virology. 1989 Jul;171(1):302-5.

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

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Department of Molecular Genetics and Microbiology, Robert Wood Johnson Medical School, University of Medicine and Dentistry, Piscataway, New Jersey 08854-5635.


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.

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