Treatment of human cells and interferon has no effect on the glycosylation of viral and cellular proteins.
The effect of interferon on the glycosylation of viral and cellular proteins was examined in human cells. Vesicular stomatitis virus released from control and interferon-treated HeLa cells was found to be equally glycosylated. Likewise, interferon treatment of RPMI 8226 cells, a human cell line secreting immunoglobulin G, had no effect on protein glycosylation. In addition, treatment with interferon of RPMI 8226 cells and of lymphoblastoid Daudi cells had no effect on the incorporation of N-acetylglucosamine into dolichol derivatives in a cell-free assay. Similar treatment of HeLa and murine L cells showed an apparent inhibition of this glycosyltransferase activity. This effect of interferon in HeLa cells could at least in part by accounted for by a high nucleotide pyrophosphatase activity, which degraded the sugar nucleotide substrate. These results indicate that interferon does not inhibit protein glycosylation in human cells.
D002478:Cells, Cultured; D006023:Glycoproteins / Q000096:biosynthesis; D006801:Humans; D007370:Interferon Type I / Q000494:pharmacology*; D007371:Interferon-gamma / Q000494:pharmacology*; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*
D006023:Glycoproteins; D007370:Interferon Type I; D014764:Viral Proteins; D007371:Interferon-gamma