Rabies virus glycoprotein. II. Biological and serological characterization
- 1 June 1977
- journal article
- research article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 16 (3) , 754-759
- https://doi.org/10.1128/iai.16.3.754-759.1977
Abstract
Purified rabies virus glycoprotein (G) was shown by complement fixation and immunodiffusion tests to be a second distinct antigen of the virus. It it the only structural protein of the virus that induces the formation of virus-neutralizing antibodies and which confers immunity to animals. When the G protein is taken as antigen, the complement fixation test can be used for the assay of virus-neutralizing antibodies. The total protective activity of the virus was recovered in the purified G protein preparation. The protective activity of G protein increased with purification: 9 ng of G protein was required to protect 50% of the mice as compared to 1.63 micrograms of the virus. Selective immunofluorescent membrane staining and immunocytolysis of rabies virus-infected cells were shown to be G protein specific. Due to its purity and potency, the G protein preparation can be considered the ideal human antirabies vaccine. ImagesThis publication has 22 references indexed in Scilit:
- Structure and Molecular Biology of Rabies VirusPublished by Springer Nature ,1976
- Lowry determination of protein in the presence of Triton X-100Analytical Biochemistry, 1975
- Laboratory techniques in rabies: methods of calculation.1973
- Isolation of a hemagglutinating, immunizing, and non-infectious subunit of the rabies virionArchiv für die gesamte Virusforschung, 1971
- ABSORPTION OF GUINEA PIG SERUM WITH AGARTransplantation, 1970
- Biochemical and biophysical studies on the nucleocapsid and on the RNA of rabies virusVirology, 1969
- Investigating the Rabies VirusNature, 1969
- Hemagglutinin of Rabies and Some Other Bullet-Shaped VirusesExperimental Biology and Medicine, 1968
- Syrian Hamster Fibroblast Cell Line BHK21 and its DerivativesNature, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951