Sensitivity to alpha/beta-interferon is independent of N-linked complex-type oligosaccharides on cell-surface-membrane glycoproteins.

Abstract

The extent of involvement of carbohydrate structures in the mechanism of action of alpha and beta-interferon (IFN-alpha, IFN-beta) is undefined. In this report we examine the role of complex-type N-linked oligosaccharides in the response to these interferons. The response of mouse leukemia L 1210S cells, grown in the presence of swainsonine, an inhibitor of Golgi mannosidase II [Tulsiani, D. R. P., Harris, T. M. and Touster, O. (1982) J. Biol. Chem. 257, 7936-7939; Elbein A. D., Solf, R., Dorling, P. R. and Vosbeck, K. (1981) Proc. Natl Acad. Sci. USA 78, 7393-7397], to mouse IFN-alpha/beta, both with respect to antiviral and antigrowth effects, remains intact in spite of the total absence of complex-type N-linked oligosaccharides. Also, there is no difference in the response to human IFN-beta of a parental Chinese hamster ovary cell line and a mutant lacking beta-N-acetylglucosaminyltransferase I and therefore unable to synthesize complex-type N-linked oligosaccharides [Stanley, P., Callibot, V. and Siminovitch, L. (1975) Cell 6, 121-128]. These results are significant in permitting the conclusion that the carbohydrate-specific binding of IFN-alpha and IFN-beta to gangliosides cannot be due to a similarity of the ganglioside carbohydrate to that of a glycoprotein containing a complex-type N-liked oligosaccharide.