Purification and characterization of the major envelope glycoprotein of simian foamy virus type 1.

Simian foamy virus type 1 (SFV-1), the prototype of the Spumavirinae, was subjected to disruption and serial purification procedures. Separation of SFV-1 envelope components from viral cores was verified by electron microscopy, density gradient centrifugation and polyacrylamide gel electrophoresis. After affinity chromatography of the envelope polypeptides on a concanavalin A-Sepharose column, a highly purified 70 000 mol. wt. protein was recovered. Glycosylation of this gp70 was confirmed by glucosamine labelling. Immunological studies with anti-SFV antisera confirmed the type-specificity of this envelope gp70.