Structure of carbohydrate part of receptor on human uroepithelial cells for pyelonephritogenic Escherichia coli.

The binding of pyelonephritogenic Escherichia coli strains to human uroepithelial cells from patients with and without P blood group antigens was investigated. Uroepithelial cells from p phenotypes bound pyelonephritogenic e. coli to a significantly lesser extent than did cells from P1 and P2 phenotypes. The binding of pyelonephritogenic E. coli to urinary epithelial cells of P1 phenotypes was blocked by the synthetic disaccharide alpha-D-Galp-(1 leads to 4)-beta-D-Galp whose structures is related to that of the P blood group antigens. Coating of P1 cells with a synthetic disaccharide derivative increased the binding of bacteria. None of 30 individuals of p phenotype had had urinary tract infection. The findings show that the disaccharide alpha-D-Galp-(1 leads to 4)-beta-D-Galp, previously shown to be the erythrocyte receptor for the fimbriae of pyelonephritongenic E. coli, is also the receptor structure on uroepithelial cells.