Rabies Virus Glycoprotein Analogs: Biosynthesis in Escherichia coli

This chapter describes the direct expression in Escherichia coli of the glycoprotein gene of rabies virus. In 1885, Louis Pasteur developed the first rabies vaccine by emulsifying desiccated spinal cords of rabies-infected rabbits. Freshly solubilized preparations of G₅₀₅ reacted with the antibody about 90 percent as effectively as natural glycoprotein, while the activities of solubilized preparations of G₄₂₇ were no higher than 70 percent those of authentic glycoprotein. Rabies glycoprotein, when removed from intact virions, is quite insoluble. The more intensely labeled bands in lanes k and l correspond with the rabies virus specific bands easily visible in stained slab gels. The full-length bacterially expressed rabies glycoprotein, termed G₅₀₅, comigrates with a major class of E. coli proteins, but can be observed as a widening of the stained protein band at about 57,000 daltons. Further purification of the G₄₂₇ and G505 proteins for in vitro competition assays with authentic rabies glycoprotein and for animal inoculation is necessary.