Clostridium botulinum type A progenitor toxin binds to Intestine-407 cells via N-acetyllactosamine moiety

  • Biochem Biophys Res Commun. 2005 Jun 3;331(2):571-6. doi: 10.1016/j.bbrc.2005.04.007.
Shoudou Kojima  1 ,  Hironobu Eguchi ,  Tomomi Ookawara ,  Noriko Fujiwara ,  Jun Yasuda ,  Kazuhiko Nakagawa ,  Takehira Yamamura ,  Keiichiro Suzuki
Affiliations
  • 1. Department of Biochemistry, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya, Hyogo 663-8501, Japan.
PMID: 15850798 DOI: 10.1016/j.bbrc.2005.04.007
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 beta-galactosidase and beta-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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