[Preparatory extraction and study of the structural proteins of rabies virus]

A technology for preparation of purified concentrates of rabies virus has been developed permitting to use simultaneously dozens of liters of tissue culture virus-containing fluid for the preparation of a concentrate. When concentrated 10(4)-fold or more, the degree of virus purification relative soluble proteins was at least 8 X 10(6). The virus yield in purified preparations was approximately 500 microgram of protein per 10 1 of the original culture fluid. Purification and preparation of a surface antigen of rabies virus, protein G, was also carried out. The yield of this protein in the resulting preparations was about 170 microgram per 10 1 of the culture fluid, the degree of purity being about 90%. A re-evaluation of the set, characteristics, and localization of rabies virus structural proteins was done. According to the experimental results, virus nucleocapsids contain 3 classes of proteins: L (a minor components with molecular weight of approximately 200,000), N (the dominating component, approximately 54,000) and NS (an intermediate component, approximately 47,000). The inner layer of virus lipoprotein membrane consists of protein M molecules (approximately 21,000) and apparently of protein A molecules (approximately 43,000) which are likely to be of cellular actin. The external spikes (peplomers) of virus particles contain molecules of glycoprotein G (approximately 65,000). Thus, the experimental results permit a conclusion that previously assumed significant differences in the protein composition of rabies viruses on the one hand and the other rhabdoviruses on the other are non-existent.