Preparation and characterization of rabies virus hemagglutinin.
Rabies virus glycoprotein, released by treatment with Triton X-100, was isoelectrically focused in a sucrose gradient containing the nonionic detergent octylglucoside. Removal of the detergent by dialysis resulted in aggregates of variable size and shape. The hemagglutinating activity of this preparation was approximately sixfold higher than that of the intact virus. The protein with hemagglutinating activity and with a buoyant density of 1.237 consisted solely of polypeptide chains of the G-protein and contained 0.38% phospholipids and 16 ng of Triton X-100 per mg of protein. In the National Institutes of Health test the hemagglutinin conferred a significantly higher protective activity than detergent-associated glycoprotein and was as effective as an inactivated virus vaccine. However, after the application of a single dose of hemagglutinin, the onset of protection was delayed by approximately 7 days when compared with inactivated virus vaccine.
D002499:Centrifugation, Density Gradient; D003902:Detergents; D004586:Electrophoresis; D006023:Glycoproteins / Q000276:immunology; D006389:Hemagglutinins, Viral / Q000032:analysis*; D008854:Microscopy, Electron; D010743:Phospholipids / Q000032:analysis; D011820:Rabies virus / Q000276:immunology* / Q000648:ultrastructure; D014764:Viral Proteins / Q000276:immunology
D003902:Detergents; D006023:Glycoproteins; D006389:Hemagglutinins, Viral; D010743:Phospholipids; D014764:Viral Proteins