[Immunization with live attenuated A/H5N1 vaccine protects guinea pigs from reinfection].

Cold-adapted influenza virus A/HK/1/68/162/35(H3N2) was developed as unified donor of attenuation and high reproductive capacity forvaccine strains. The reassortant of this donor with surface antigens of highly pathogenic strain Alchicken/Astana/6/05 (H5N1) was tested in guinea pigs as a live or inactivated preparation. Immunization with both formulations induced equal levels of serum virus specific antibodies, while the level of mucosal antibodies was significantly higher in animals immunized with live virus.

[The influenza viruses and their surface proteins impact on the metabolism of human blood vessel endothelium cells].

The modern influenza virus subtypes H3N2, H5N1, and H1N1 reduced the metabolism of the endothelial cells within the range from 20% to 60% (compared with control). The degree of the activity of the dehydrogenase reduction depended on the dose of virus and time of virus reproduction. HA and NA also actively reduced the metabolism of the cells ranging from 5% to 60%, depending on the concentration of the proteins and time of their impact on cells.

[Formation of antibodies against neuraminidase of A/California/07/2009 (H1N1) influenza virus after immunization with live monovalent influenza vaccine].

Aim: Detection of antibodies against neuraminidase (NA) of A/California/07/2009 (H1N1) influenza virus in blood sera of volunteers after the immunization with live monovalent influenza vaccine (LIV).

Materials And Methods: Neuraminidase enzyme activity inhibition by antibodies test with reassortant strain A(H7N1) containing NA of pandemic strain was used. Anti-neuraminidase IgG antibodies against whole reassortant virus A(H7N1) and purified NA of A/California/07/2009 (H1N1) strains were determined by enzyme immunoassay (EIA).

[Purification and properties of copper thionein].

A novel procedure for purification of copper-thionein from rabbit liver was developed. The molecular mass, copper, and thiol contents were determined. The properties of the protein were compared with those of Cd-thionein.