摘要:Extracts of uroepithclial cells from healthy female individuals, prepared in phosphate-buffered saline containing EDTA, 2-mercaptoethanol and lactose yielded lectin-like proteins which haemagglutinated human ARh- erythrocytes and which were specifically inhibited by galactose, lactose and hog-gastric mucin. Affinity chromatography of uroepithelial extracts using mucin-Sepharose and elution in the presence of galactose or lactose resulted in the isolation of a group of polypeptides ranging in M, from 55 000 to 67 000 Da as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis. Preincubation of three female urinary tract bacterial isolates, Staphylococcus saprophyticus, Lactobacillus sp. and Bacteroides intermedius, with these proteins resulted in significantly (P < 0.001) decreased adherence of these isolates to uroepithelial cells as tested in an in vitro assay system. These data suggest presence of endogenous lectin activity associated with human uroepithelial cells which may influence the adhesion of commensal or pathogenic urinary flora.Keywords: Uroepithelium; Lectin; Bacterial adherence.