FimH is the type 1 fimbrial tip adhesin and invasin of Escherichia coli. Its ligands are the glycans on specific proteins enriched in membrane microdomains. FimH binding shows high-affinity recognition of paucimannosidic glycans, which are shortened high-mannose glycans such as oligomannose-3 and -5. FimH can recognize equally the (single) high-mannose glycan on uroplakin Ia, on the urinary defence protein uromodulin or Tamm–Horsfall glycoprotein and on the intestinal GP2 glycoprotein present in Peyer's patches. E. coli bacteria may attach to epithelial cells via hundreds of fimbriae in a multivalent fashion. This binding is considered to provoke conformational changes in the glycoprotein receptor that translate into signalling in the cytoplasm of the infected epithelial cell. Bladder cell invasion by the uropathogenic bacterium is the prelude to recurrent and persistent urinary tract infections in humans. Patients suffering from diabetes mellitus are more prone to contract urinary tract infections. In a study of women, despite longer treatments with a more potent antibiotic, these patients also have more often recurrences of urinary tract infections compared with women without diabetes. Type 1 fimbriae are the most important virulence factors used not only for adhesion of E. coli in the urinary tract, but also for the colonization by E. coli in patients with Crohn's disease or ulcerative colitis. It appears that the increased prevalence of urinary tract infections in diabetic women is not the result of a difference in the bacteria, but is due to changes in the uroepithelial cells leading to an increased adherence of E. coli expressing type 1 fimbriae. Hypothetically, these changes are in the glycosylation of the infected cells. The present article focuses on possible underlying mechanisms for glycosylation changes in the uroepithelial cell receptors for FimH. Like diabetes, bacterial adhesion induces apoptosis that may bring the endoplasmic reticulum membrane with immature mannosylated glycoproteins to the surface. Indicatively, clathrin-mediated vesicle trafficking of glucose transporters is disturbed in diabetics, which would interfere further with the biosynthesis and localization of complex N-linked glycans.
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February 2011
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Conference Article|
January 19 2011
Glycosylation changes as important factors for the susceptibility to urinary tract infection
Joemar Taganna;
Joemar Taganna
*Unit for Molecular Glycobiology, VIB Department for Molecular Biomedical Research, Ghent University, Technologiepark 927, 9052 Ghent, Belgium
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Arjen R. de Boer;
Arjen R. de Boer
†Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands
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Manfred Wuhrer;
Manfred Wuhrer
†Biomolecular Mass Spectrometry Unit, Department of Parasitology, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands
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Julie Bouckaert
Julie Bouckaert
1
‡Laboratoire de Glycobiologie Structurale et Fonctionnelle, UMR 8576 du CNRS, UFR de Biologie, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France
1To whom correspondence should be addressed (email julie.bouckaert@univ-lille1.fr).
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Publisher: Portland Press Ltd
Received:
November 09 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (1): 349–354.
Article history
Received:
November 09 2010
Citation
Joemar Taganna, Arjen R. de Boer, Manfred Wuhrer, Julie Bouckaert; Glycosylation changes as important factors for the susceptibility to urinary tract infection. Biochem Soc Trans 1 February 2011; 39 (1): 349–354. doi: https://doi.org/10.1042/BST0390349
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