Saccharomyces boulardii inhibits Clostridium difficile toxin A binding and enterotoxicity in rat ileum

• Published in: Gastroenterology (New York, N.Y. 1943) Vol. 104; no. 4; p. 1108
• Main Authors: Pothoulakis, C, Kelly, C P, Joshi, M A, Gao, N, O'Keane, C J, Castagliuolo, I, Lamont, J T
• Format: Journal Article
• Language: English
• Published: United States 01-04-1993
• Subjects: Animals; Bacterial Toxins - metabolism; Bacterial Toxins - toxicity; Chromatography, Affinity; Clostridium difficile; Electrophoresis, Polyacrylamide Gel; Enterotoxins - metabolism; Enterotoxins - toxicity; Ileum - drug effects; Ileum - metabolism; Ileum - pathology; Male; Mannitol - metabolism; Membrane Proteins - isolation & purification; Membrane Proteins - metabolism; Microvilli - drug effects; Microvilli - metabolism; Microvilli - ultrastructure; Molecular Weight; Rabbits; Rats; Rats, Wistar; Receptors, Immunologic - isolation & purification; Receptors, Immunologic - metabolism; Saccharomyces; Tritium
• ISSN: 0016-5085
• DOI: 10.1016/0016-5085(93)90280-p

Saccharomyces boulardii is a nonpathogenic yeast used for the prevention and treatment of Clostridium difficile-associated diarrhea and colitis. However, the mechanism by which S. boulardii exerts its protective effects remains unclear.
The binding of [3H]toxin A to its brush border receptor preincubated with S. boulardii-cultured suspension or filtered conditioned medium was measured in vitro. The effect of toxin A on secretion, epithelial permeability, and morphology in rat ileal loops in vivo was also examined in rats pretreated with S. boulardii.
S. boulardii reduced [3H]toxin A-receptor binding in a dose-dependent fashion. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of ileal brush border exposed to S. boulardii-conditioned medium revealed a diminution of all brush border proteins. Treatment of rats with S. boulardii suspension reduced fluid secretion and mannitol permeability caused by toxin A.
S. boulardii may reduce some of the enterotoxic effects of toxin A by inhibiting toxin A-receptor binding. This effect appears to be manifested by a secreted product of the yeast, possibly a protease.