The relationship of the influenza virus inhibitory activity of glycoproteins to their molecular size and sialic acid content.
Twenty-four different glycoproteins were investigated for their ability to inhibit hemagglutination by the A/PRS and the B/Md influenza virus strains. A relationship between activity, the molecular size, and sialic acid content was found. This relationship was readily shown for the A/PR8 virus if the properties of the glycoproteins were compared with one another on a per cent basis. A proportion of approximately 1:1:1 for activity (weight basis) to moles sialic acid content to molecular weight existed for each inhibitory glycoprotein with more than 3 per cent sialic acid, on comparison with any other active glycoprotein.A 1:3 correspondence between viral subunit and sialic acid residues of the inhibitor ovine submaxillary mucin was found experimentally and confirmed by calculation on a molecular model. The most potent inhibitors, were the antigens of the human blood-group MN system and the Tamm-Horsfall urinary glycoprotein.
D006023:Glycoproteins / Q000494:pharmacology*; D006385:Hemagglutination Inhibition Tests; D007120:Immunochemistry; D008970:Molecular Weight; D009438:Neuraminic Acids / Q000032:analysis*; D009975:Orthomyxoviridae / Q000187:drug effects*
D006023:Glycoproteins; D009438:Neuraminic Acids