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Influenza B viruses isolated in 1940, 1950 and 1970 belonged to antigenically remote subgroups according to the antigenic composition of haemagglutinin (HA). Antigenically related strains isolated in 1972-1976 differed by their reproduction capability, by their sensitivity to inhibitors in mammalian sera and by affinity to specific antibodies in human sera. Certain correlation between these properties was observed by strains of the Hong Kong variant. Polyacrylamide gel electrophoresis (PAGE) showed that the viruses under study differed in the mobility of the major HA chain (HA1). Molecular weights (MW) of HA1 of antigenically similar influenza B viruses isolated in 1972-1976 revealing different biological properties varied from 52.5 K to 58 K. Neuraminidase (NA) of influenza B/Leningrad/369/75 virus purified by electrophoresis in acetate cellulose consisted of 2 polypeptides with apparent MW of 62 K and 57 K. All viruses examined showed similar mobility of the NA polypeptide MW 57 K; the mobility of the former polypeptide was similar to that of nucleoprotein (NP).

The reproduction patterns of various influenza B virus strains isolated in 1970-1976 using roller cultures of MDCK cells and chick embryos (CE) were compared. The cultural and allantoic virus populations did not differ in their sensitivity to non-specific inhibitors from mammalian sera and in their reactivity with specific haemagglutinins (HA). The content of infectious virus and HA in the harvested allantoic fluids as compared to medium fluids were 94- and 8-fold higher, respectively, even though the fluids did not differ in the titres of complement-fixing (CF) antigen. The mol. weight (MW) of HA1 polypeptide of the B/Len/75 virus prepared in culture was higher than that Of the allantoic virus (57.5 K and 55.5 K, respectively). Under reducing conditions, the HA of the virus from culture was represented mostly by the uncleaved HA0 polypeptide, while that of the allantoic virus by the HA1 and HA2 subunits. Under non-reducing conditions, the virus from medium fluid was found to contain glycopeptide D with MW of 90 K.