[Antigenic and biological characteristics of influenza virus A strains isolated in 1985].

The antigenic structure of hemagglutinin of influenza A virus (H3N2) strains isolated in 1985 was studied using a series of monoclonal antibody to A/Dunedin/4/73/A (H3N2) and A/Bangkok/1/79/A (H3N2), and biological and physico-chemical properties of these strains were compared with those of influenza A (H3N2) virus of 1983 and reference A (H3N2) of 1979-1984 (the rate of adsorption on chick erythrocytes and eluting activity, thermostability of hemagglutinin and neuraminidase, sensitivity to nonionic detergents, sensitivity to remantadine, analysis of virion polypeptide composition). A high degree of heterogeneity of the 1985 strain population of influenza A (H3N2) virus was revealed both in the antigenic structure of hemagglutinin and in all the biological and physico-chemical parameters tested. It was suggested that the A/Caen/1/84 strain originated not from A/Philippines/2/82 but directly from A/Texas/1/77.

[Analysis of the antigenic specificity of the neuraminidases of influenza B viruses isolated in different years].

The antigenic structure of neuraminidases of influenza B viruses isolated in 1940-1984 was studied. Lectin test has first been employed for analysis of influenza B virus neuraminidase. The antigenic composition of neuraminidases of these viruses was shown to be different.

[Antigenic specificity of the neuraminidases of epidemic strains of influenza A/H3N2 viruses circulating in the USSR 1983-1985].

The antigenic properties of neuraminidase of the epidemic strains of 1983-1985 were studied by means of lectin test and thiobarbituric method using polyclonal sera and monoclonal antibody. Populations of the viruses with respect to antigenic relationships of neuraminidase were shown to be heterogeneous. A considerable portion of the strains occurring in 1985 underwent antigenic drift from the reference A/Philippines/2/82 strain.

[Isolation and study of the properties of IgG from antisera to influenza virus proteins].

IgG to internal (NP, M) and external (HA, NA) proteins of influenza virus were isolated from immune rabbit sera using caprylic acid. The IgG retained their specificity and activity, worked in HI, lectin test, and enzyme-immunoassay. IgG migrated towards cathode in electrophoresis on acetate cellulose.

[Biological consequences of breaks and reunions of disulfide bonds in influenza virus proteins].

Consequences of chemical breakage of native disulphide bonds in influenza virus neuraminidase and hemagglutinin glycoproteins induced by mercaptoethanol treatment were studied. Under conditions of blocked reoxidation of thiol groups, this treatment led to significant inhibition of hemagglutinating activity and infectivity of virus particles, and to a lesser inhibition of neuraminidase activity, as well as to promotion of endogenous proteolytic activity. Analysis of virus particles proteins by polyacrylamide gel electrophoresis indicated association of these biological effects with breakage of disulphide bridges, mainly in hemagglutinin glycoproteins.