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Papers In Press, published online ahead of print March 4, 2002
Institute of Medical Biochemistry, Goteborg University, Göteborg SE 405 30
Corresponding Author: Susann.Teneberg{at}medkem.gu.se
Bacterial adherence to mucosal cells is a key virulence trait of pathogenic bacteria. The type 1 fimbriae and the P-fimbriae have both been described to be important for the establishment of urinary tract infections. While P-fimbriae recognize kidney glycosphingolipids carrying the Gala4Gal-determinant, type 1 fimbriae bind to the urothelial mannosylated glycoproteins uroplakin Ia and Ib. The F1C fimbriae are one additional type of fimbriae correlated with uropathogenicity. Although it was identified 20 years ago its receptor has remained unidentified. Here we report that F1C-fimbriated bacteria selectively interact with two minor glycosphingolipids isolated from rat, canine and human urinary tract. Binding-active compounds were isolated and characterized as galactosylceramide, and globotriaosylceramide, both with phytosphingosine and hydroxy fatty acids. Comparison with reference glycosphingolipids revealed that the receptor specificity is dependent on the ceramide composition. Galactosylceramide was present in the bladder, urethers, and kidney while globotriaosylceramide was present only in the kidney. Using a functional assay, we demonstrate that binding of F1C fimbriated E. coli to renal cells induces IL-8 production, thus suggesting a role for F1C-mediated attachment in mucosal defence against bacterial infections.
J. Biol. Chem, 10.1074/jbc.M111640200
Submitted on December 6, 2001
Revised on March 4, 2002
Accepted on March 3, 2002
Identification of target tissue glycosphingolipid receptors for uropathogenic, F1C-fimbriated Escherichia coli and its role in mucosal inflammation
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