Glycolipid modification of alpha 2 interferon binding. Sequence similarity between the alpha 2 interferon receptor and verotoxin (Shiga-like toxin) B-subunit.

Previous studies have implicated the glycolipid receptor for the Escherichia coli-derived verotoxin, globotriaosylceramide (Gb3; Gal alpha 1-4Gal beta 1-4Glc-ceramide), in the mechanism of alpha 2 interferon signal transduction. Comparison of the amino acid sequence of the human alpha 2 interferon receptor with that of the B (receptor-binding)-subunit of verotoxin shows three regions of similarity which may provide a structural basis for alpha 2-interferon-receptor/Gb3 interaction.