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.
Animals Antibodies, Monoclonal