Abstract
The bifunctional reagent dimethylsuberimidate was used to cross-link the proteins in: (1) intact Semliki Forest virus (SFV); (2) SFV containing a small amount of the detergent Triton X-100; (3) detergent released SFV membranes; (4) membranes solubilized with Triton X-100 into lipoprotein-detergent complexes; and (5) membranes solubilized into lipid-free glycoprotein-detergent complexes. Analyses of the cross-linked glycoprotein polymers by SDS gel electrophoresis showed that the two 50,000 molecular weight (MW) glycoproteins E1 and E2 of the SFV membrane were preferentially cross-linked into dimers in all preparations. This suggests that oligomeric glycoprotein units, containing two 50,000 MW glycoproteins, are present in the viral membrane and that these remain associated with each other when solubilized with Triton X-100.
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