Participation of ABH glycoconjugates in the secretory response to Escherichia coli heat-labile toxin in rabbit intestine

GALVAN EM, ROTH GA, MONFERRAN CG

The Infectious Diseases Society of America

Año: 1999 vol. 180 p. 419 - 419

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt; tab-stops: 21.3pt">The ability of membrane ABH blood group-active glycoconjugates to act as receptors of the heat-labile toxin from Escherichia coli isolated from human (LTh) was studied in vitro and in vivo when GM1 was blocked by the cholera toxin B subunit. Rabbits were classified as AB or H based on intestinal ABH-antigenic activities. Brush border membranes from AB rabbits contained 4 times more LTh binding sites than the H ones. LTh interaction could be inhibited by  lectins that recognize ABH-blood group determinants. LTh induced similar dose-dependent secretory response in ligated ileal loops of