Interaction of cholera toxin and Escherichia coli heat-labile enterotoxin with glycoconjugates form rabbit intestinal brush border membranes: Relationship with ABH blood goup determinants

LE BALANZINO, JL BARRA, EM GALVAN, GA ROTH, CG MONFERRAN

Kluwer Academic Publishers

Año: 1999 vol. 194 p. 53 - 53

je capacity of cholera toxin (CT) and type I heat-labile enterotoxin produced by Escherichia coli isolated from human intestine (LTh) to  interact with clydoconjugates bearing ABH blood group determinants  form rabbit intestinal brush border membranes  (BBM) was studied. On the basis of the type of intestinal compounds related to the human ABH blood group antigens, rabbits were classified as AB or H. Toxin binding to intestinal glycolipids and glycoproteins depends on the blood group determinant borne by the glycoconjugate and on the analyzed toxin. LTh was capable of interacting preferentially with  several blood group A and B-active BBM glycolipids compared to those isolated from animals lacking these antigens (H rabbits). Also, LTh preferably bound to several BBM glycoproteins from AB rabbit intestines compared to those form H ones. One of these glycoproteins, the sucrase-isomaltase complex (EC 3.2.1.48-10) isolated from AB and H rabbits showed the same diffenti