Effect of glycolipids and glycophorin on the activity of human interferon-beta and -gamma.
We have studied neutralization of the antiviral activity of human fibroblast (IFN-beta) and immune interferon (IFN-gamma) by incubation with glycolipids (including the gangliosides GM1, GM2 and GM3, as well as various other glycolipids) and with the sialoglycoprotein, glycophorin. When 100 units/ml of IFN-beta were preincubated with 30-80 microM of the gangliosides, all antiviral activity was abolished. Similarly, 120 microM of glycophorin completely reversed the antiviral activity of 100 units/ml of IFN-beta. Glycolipids containing more than two sugars also showed moderate inhibitory effects. GM2 at a concentration of 200 microM almost completely inhibited the antiviral activity of 100 units/ml of IFN-gamma, but GM1, GM3 and glycophorin had only a moderate inhibitory effect. These results suggest that the terminal N-acetylneuraminic acid (NANA) residues of gangliosides and of glycophorin play an important role in the inhibition of IFN-beta, and that they may be similarly involved in the inhibition of IFN-gamma.
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D005732:Gangliosides / Q000494:pharmacology; D006017:Glycolipids / Q000494:pharmacology*; D006021:Glycophorins / Q000494:pharmacology*; D006801:Humans; D007370:Interferon Type I / Q000037:antagonists & inhibitors* / Q000378:metabolism; D007371:Interferon-gamma / Q000037:antagonists & inhibitors* / Q000378:metabolism; D012794:Sialic Acids / Q000494:pharmacology; D012795:Sialoglycoproteins / Q000494:pharmacology*; D013329:Structure-Activity Relationship
D005732:Gangliosides; D006017:Glycolipids; D006021:Glycophorins; D007370:Interferon Type I; D012794:Sialic Acids; D012795:Sialoglycoproteins; D007371:Interferon-gamma