Open AccessPreparation and characterization of rabies virus hemagglutinin
Author(s) -
James H. Cox,
Bernhard Dietzschold,
Frank Weiland,
Lothar Schneider
Publication year - 1980
Publication title -
infection and immunity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.508
H-Index - 220
eISSN - 1070-6313
pISSN - 0019-9567
DOI - 10.1128/iai.30.2.572-577.1980
Subject(s) - hemagglutinin (influenza) , virus , biology , rabies virus , virology , glycoprotein , rabies , microbiology and biotechnology
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.