Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10769989 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
Botulism is a highly fatal disease caused by the botulinum progenitor toxin. In this study, the role of oligosaccharides for the binding of botulinum type A progenitor toxin (type A PTX) to human intestinal cells was investigated. The binding of type A PTX to Intestine-407 cells was inhibited by the addition of N-acetyllactosamine, lactose, and galactose. Treatment of Intestine-407 cells with neuraminidase led to a significant increase in the binding of type A PTX, while further digestion of cell surface oligosaccharides by β-galactosidase and β-N-acetylhexosaminidase decreased the binding. These results indicate that the N-acetyllactosamine moiety is responsible for the binding of type A PTX. These findings were further confirmed by a binding assay using synthesized oligosaccharides. Interestingly, sialylation or fucosylation of oligosaccharides inhibited the binding of type A PTX. These data suggest that the type A PTX binds to intestinal cells via cell surface N-acetyllactosamine moiety.
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Authors
Shoudou Kojima, Hironobu Eguchi, Tomomi Ookawara, Noriko Fujiwara, Jun Yasuda, Kazuhiko Nakagawa, Takehira Yamamura, Keiichiro Suzuki,