Preparation and characterization of rabies virus hemagglutinin

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Abstract
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 .apprx. 6-fold 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/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. After the application of a single dose of hemagglutinin, the onset of protection was delayed by .apprx. 7 days when compared with inactivated virus vaccine.