[Isolation of monoclonal antibodies for the identification of strains of the causative agent of plague that do not contain a capsular antigen]. / Poluchenie monoklonal'nykh antitel dlia identifikatsii shtammov vozbuditelia chumy, ne soderzhashchikh kapsul'nogo antigena.

In most cases the immunological identification of Y. pestis strains is based on the use of capsular antigen as an immunological marker. However, there are Y. pestis strains without capsular antigen. For the immunological identification of such strains, homogeneous antigen with a molecular weight of 43 KD has been isolated and monoclonal antibodies to it have been obtained. The enzyme-linked immunosorbent assay, carried out with the use of these monoclonal antibodies and intended for the detection of antigen with a molecular weight of 43 KD, has been developed. The sensitivity of the assay is about 10 ng/ml.

[Radioimmunological analysis of the antigenic variability of influenza virus nucleoprotein]. / Radioimmunologicheskii analiz antigennoi variabel'nosti nukleoproteina virusa grippa.

Influenza A virus ability to bind anti-NP monoclonal antibodies to two viral strains has been studied by radioimmunoassay on polyethylene film with the subsequent autoradiographic registration of results. Monoclonal antibodies were obtained to the viral strains differing in antigenic formula of outer glycoproteids and isolated at different time. The studied influenza viruses were divided into seven groups due to their ability to bind monoclonal antibodies. The absence of correlation between the antigenic properties of nucleoprotein and glycoproteids has been registered. Variability of some antigenic sites has been analyzed. The human epidemic strains of influenza virus are different in ability to bind monoclonal antibodies from the viral strains that are connected with animals in nature or laboratory practice.

[Study of the host glycosyl component of the influenza virus using monoclonal antibodies]. / Izuchenie glikozil'nogo khoziaiskogo komponenta virusa grippa s ispol'zovaniem monoklonal'nykh antitel.

The crossreacting glycosylated host component (COHC) of influenza virus propagated in chick embryo has been studied using the monoclonal antibodies (MA). The specificity of MA to COHC has been demonstrated by different methods. Both MA of clones A9 and B7 react with the spatially overlapping antigenic sites of oligosaccharide chain, but only MA of B7 are active in hemagglutination inhibition test. The COHC is shown to be associated with both surface glycoprotein adsorbing on the surface of the virion. The study of the components from the allantonic fluid has shown the COHC to be associated with the sole embryo glycoprotein with the mol. mass around 150 kD and p1 9.0-9.5. Thus, the glycoprotein is possibly identical with the glycoprotein adsorbing on the virion surface. The content of COHC in various preparations of influenza virions has been also studied. The relative content of COHC is shown to increase during the purification of viral preparation. The COHC effect on the characteristics of vaccine preparations is discussed.

[Monoclonal antibodies to NP protein and their use in studying influenza A viruses]. / Monoklonal'nye antitela k NP-belku i ikh ispol'zovanie dlia izucheniia virusov grippa A.

Monoclonal antibodies to NP-proteins of influenza A/sea gull/Kazakhstan/470/79 (H1N1) virus have been prepared. Each clone interacted with spatially non-overlapping antigenic sites of NP-protein. The clones differed in their capacity to inhibit the polymerase activity of different influenza A virus strains. F-81 clone was shown to interact actively with NP of human influenza A viruses, clone H12 reacted with both human and animal influenza viruses.