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Journal of Medical Microbiology logo Journal of Medical Microbiology

Volume 46, Issue 11

toxin A binding to human intestinal epithelial cells No Access

Abstract

radiolabelled toxin A ([H]-toxin A) bound to human duodenal and colonic epithelial cells isolated from endoscopic biopsies. Binding was greater at 4°C than 37°C, consistent with the thermal binding characteristic of toxin A to a carbohydrate moiety. At 37°C colonic cells bound significantly more [3H]-toxin A than duodenal cells. The amount of [3H]-toxin A binding varied considerably between individuals. [H]-toxin A was displaced by unlabelled toxin A by 50% for duodenal cells and 70% for colonic cells with 94.3 nM unlabelled toxin A. Low non-displacable binding was observed in some samples at 4°C and 37°C, suggesting that these cells came from individuals incapable of specifically binding toxin. Pre-treating cells with - or -galactosidases to cleave terminal - and -galactose residues reduced [3H]-toxin A binding. There was also a reduction in [H]-toxin A binding after heat treating cells, which is suggestive of protein binding. The reduction in binding varied between individuals. The reduction of [H]-toxin A binding, after the removal of -linked galactose units, implicates these as components of the receptor and adds credence to the idea that the Lewis X, Y and I antigens may be involved in toxin A binding to human intestinal epithelial cells. However, because the Lewis antigens do not possess terminal -galactose units, the reduction in binding after -galactosidase treatment suggests that other receptors may be involved in toxin A binding to some human intestinal cells. These data are the first demonstration of direct toxin A binding to human intestinal epithelial cells.

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© 1997 The Pathological Society of Great Britain and Ireland
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1997-11-01
2025-01-16
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/content/journal/jmm/10.1099/00222615-46-11-953
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Clostridium difficile toxin A binding to human intestinal epithelial cells
J. Med. Microbiol. 46, 953 (1997); https://doi.org/10.1099/00222615-46-11-953
/content/journal/jmm/10.1099/00222615-46-11-953
/content/journal/jmm/10.1099/00222615-46-11-953
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