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Heterogeneity of Sindbis Virus Glycoprotein E₁ and its Modification by Host Cell Transformation

Department of Microbiology, School of Medicine, Chiba University, Inohana, Chiba, Chiba 280, Japan

The electrophoretic properties of glycoprotein E₁ of Sindbis virus grown in Rous sarcoma virus-transformed cells were compared with those of Sindbis virus grown in untransformed cells. Isoelectric focusing in a gel containing 9.5 M-urea and 2% Nonidet P40 indicated that the glycoprotein E₁ of Sindbis virus from the untransformed cells was electrochemically heterogeneous and consisted of four components, whose isoelectric points (pIs) ranged from 6.2 to 6.7; the E₁ of Sindbis virus from the transformed cells contained an additional component with a pI of 6.1. After treatment with neuraminidase the observed charge heterogeneity disappeared regardless of whether the virus had come from the transformed or the untransformed cells. The five components were digested with Pronase and compared by gel filtration on Bio-Gel P-6; the four components with relatively higher pIs released high-mannose-type and complex-type oligosaccharides which differed in their content of sialic acid. In contrast, the pI 6.1 component, which existed only in the transformed cell-derived SV glycoprotein E₁, released only complex-type oligosaccharide. These results indicate that the properties of glycoprotein E₁ derived from both cell types are basically similar but that a small proportion of the E₁ molecules from the transformed cells, with carbohydrate chains elongated by attachment of sialic acid residues, lacks simple-type oligosaccharides either because they are not attached or because they have been processed to the complex type. Glycoprotein E₂ appeared as at least three components in nonequilibrium pH gradient electrophoresis. However, no significant difference was observed between the cell types.

Keywords: Sindbis virus, Rous sarcoma virus, glycoprotein, transformation

Received 29 June 1983; accepted 17 October 1983.

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