Restoration of specific myxovirus receptors to asialoerythrocytes by incorporation of sialic acid with pure sialyltransferases.

摘要: Removal of sialic acids from human erythrocytes with Vibrio cholera neuraminidase abolished hemagglutination by two paramyxoviruses, Sendai and Newcastle disease, orthomyxoviruses, a influenza A2 virus (Japan/305/57), an equine A (Equine i/Prague/56). Selective replacement acid in the sequences NeuAccu2 + 6 Gal, NeuAca2 -+ GGalNAc, or NeuAccv2 3Gal was accomplished three different homogeneous sialyltransferases, each which is specific for synthesis one these structures. Hemagglutination titers were restored to original levels all four viruses incorporation about 40% content native cells fl-galactoside a2 3 sialyltransferase. This enzyme has strict acceptor substrate specificity Galfll 3GalNAcal 0-Thr/Ser sequence found asialoglycophorin, major erythrocyte glycoprotein, forms structure NeuAccvt 3Gal/31+ 0-Thr/Ser. Analysis labeled proteins sodium dodecyl sulfategel electrophoresis showed that 85 90% [l’C]NeuAc incorporated into co-migrated glycophorin. Incorporation other sialyltransferases did not result Sendai, viruses. In contrast, both virus. Thus, attachment 6Gal NeuAccvP 6GalNAc restores receptor sites only myxoviruses examined.