Chemical and clinical studies on the interaction of Escherichia coli with host glycolipid receptors in urinary tract infection.

The role of glycosphingolipids as host receptors, and fimbriae as bacterial ligands, for the adhesive and hemagglutinating reactions of uropathogenic E. coli was assessed. Glycolipids including globotetraosylceramide and globotriaosylceramide, which contain the disaccharide Gal alpha 1 leads to 4Gal were bound by many strains isolated from patients with pyelonephritis and cystitis. The fimbriae of one strain were shown to serve as ligands for these receptors. Although most pyelonephritic E. coli recognized globotetraosylceramide, as measured by the agglutination of glycolipid coated erythrocytes, some also recognized D-mannose residues (i.e. mannose-sensitive hemagglutination). Several strains were exclusively mannose-sensitive or bound neither globotetraosylceramide nor mannose. A genetic basis for susceptibility to infection was indicated. The erythrocytes of blood group P2 have lower amounts of Gal alpha 1 leads to 4Gal containing glycolipids than individuals of blood group P1. Blood group P2 was significantly less frequent (1/28) among patients with recurrent urinary tract infection compared to the normal population (10/40, p less than 0.02). Therefore, globoseries glycolipids may be determinants of susceptibility to urinary tract infection.