A human antibody binds to alpha-galactose receptors and mimics the effects of Clostridium difficile toxin A in rat colon

Gastroenterology
C PothoulakisJ T LaMont

Abstract

Nearly all human sera contain an immunoglobulin G antibody (antigalactose) that binds the trisaccharide Gal alpha 1-3Gal beta 1-4GlcNAc expressed on cells from most mammals but not humans. Because the Clostridium difficile toxin A receptor in rodents contains this trisaccharide, the aim of this study was to examine whether antigalactose could mimic the enterotoxic effects of toxin A and bind to receptors containing this trisaccharide. Fluid secretion, [3H]-mannitol permeability, and release of rat mast cell protease II and prostaglandin E2 were measured after luminal exposure of rat colon to either purified human anti-galactose, control immunoglobulin G, toxin A, or buffer. Toxin A (5 micrograms) and antigalactose (250 micrograms) but not control immunoglobulin (250 micrograms) stimulated colonic fluid secretion and caused increased mannitol permeability and rat mast cell protease II release. Antigalactose and toxin A and, to a lesser degree, control immunoglobulin G also stimulated release of prostaglandin E2, but only toxin A produced acute inflammation of rat colonic mucosa. Antigalactose and toxin A bound specifically to a single class of colonic brush border receptors with dissociation constants of 10(-6) mol/L and 5.4 x 1...Continue Reading

Citations

Apr 1, 2020·American Journal of Physiology. Gastrointestinal and Liver Physiology·Melinda A EngevikJames Versalovic
Dec 14, 2005·Proceedings of the National Academy of Sciences of the United States of America·Jason G S HoKenneth K-S Ng
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Feb 5, 2000·The Journal of Immunology : Official Journal of the American Association of Immunologists·H StubbeB Corthésy
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May 4, 2002·Clinical Immunology : the Official Journal of the Clinical Immunology Society·Mariadomenica D'AlessandroVincenzo Speranza
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