[Characteristics of the glycoproteins of vaccinal strains of the influenza viruses solubilized by octyl-beta-D-glucopyranoside].

The use of a nonionic detergent, octyl-beta-d-glucopyranoside (OG), under optimal conditions is highly effective in selective solubilization of membrane proteins (glycoproteins) of influenza A and B viruses, including the strains currently recommended for polytype inactivated influenza vaccines. The yield of hemagglutinin was 84-90% of the initial level in the virion concentrate. The antigenic stability of hemagglutinin of the A/H3 subtype upon storage for over 2 years and the A/H1 subtype for about 1 year (the observation period) was demonstrated. According to the results of electron microscopic studies, the glycoproteins solubilized with OG are present before removal of the detergent in the form of isolated subunits, "rosettes", and their agglomerates, and after removal of the detergent in the form of virosomes (clumps of subunits on liposomes) more heterogeneous in size (20 to 130 nm) and shape than the intact virus. The process of virosome formation is reversible and depends on the presence of the detergent. The resulting glycoproteins of influenza virus vaccine strains solubilized with the OG detergent possess the characteristics which make this agent promising for use in the manufacture of polytype subunit vaccine.