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Glycosylation changes as important factors for the susceptibility to urinary tract infection

Joemar Taganna UGent, Arjen R de Boer, Manfred Wuhrer and Julie Bouckaert (2011) BIOCHEMICAL SOCIETY TRANSACTIONS. 39(1). p.349-354
abstract
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 la, on the urinary defence protein uromodulin or Tamm-Horsfall glycoprotein and on the intestinal GP2 glycoprotein present in Peyer's patches. E. coil 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. coil 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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
FimH, diabetes mellitus, apoptosis, adhesion, paucimannosidic glycan, urinary tract infection, UROPATHOGENIC ESCHERICHIA-COLI, APOPTOTIC CELLS, UROPLAKIN-IA, UROTHELIAL RECEPTOR, STRUCTURAL BASIS, N-GLYCOSYLATION, FIMH ADHESIN, BINDING, GLYCOPROTEIN, BLADDER
journal title
BIOCHEMICAL SOCIETY TRANSACTIONS
Biochem. Soc. Trans.
volume
39
issue
1
pages
349 - 354
Web of Science type
Article
Web of Science id
000287438000064
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
3.711 (2011)
JCR rank
94/286 (2011)
JCR quartile
2 (2011)
ISSN
0300-5127
DOI
10.1042/BST0390349
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2940367
handle
http://hdl.handle.net/1854/LU-2940367
date created
2012-06-27 15:25:03
date last changed
2012-07-09 15:51:48
@article{2940367,
  abstract     = {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 la, on the urinary defence protein uromodulin or Tamm-Horsfall glycoprotein and on the intestinal GP2 glycoprotein present in Peyer's patches. E. coil 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. coil 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.},
  author       = {Taganna, Joemar and de Boer, Arjen R and Wuhrer, Manfred and Bouckaert, Julie},
  issn         = {0300-5127},
  journal      = {BIOCHEMICAL SOCIETY TRANSACTIONS},
  keyword      = {FimH,diabetes mellitus,apoptosis,adhesion,paucimannosidic glycan,urinary tract infection,UROPATHOGENIC ESCHERICHIA-COLI,APOPTOTIC CELLS,UROPLAKIN-IA,UROTHELIAL RECEPTOR,STRUCTURAL BASIS,N-GLYCOSYLATION,FIMH ADHESIN,BINDING,GLYCOPROTEIN,BLADDER},
  language     = {eng},
  number       = {1},
  pages        = {349--354},
  title        = {Glycosylation changes as important factors for the susceptibility to urinary tract infection},
  url          = {http://dx.doi.org/10.1042/BST0390349},
  volume       = {39},
  year         = {2011},
}

Chicago
Taganna, Joemar, Arjen R de Boer, Manfred Wuhrer, and Julie Bouckaert. 2011. “Glycosylation Changes as Important Factors for the Susceptibility to Urinary Tract Infection.” Biochemical Society Transactions 39 (1): 349–354.
APA
Taganna, J., de Boer, A. R., Wuhrer, M., & Bouckaert, J. (2011). Glycosylation changes as important factors for the susceptibility to urinary tract infection. BIOCHEMICAL SOCIETY TRANSACTIONS, 39(1), 349–354.
Vancouver
1.
Taganna J, de Boer AR, Wuhrer M, Bouckaert J. Glycosylation changes as important factors for the susceptibility to urinary tract infection. BIOCHEMICAL SOCIETY TRANSACTIONS. 2011;39(1):349–54.
MLA
Taganna, Joemar, Arjen R de Boer, Manfred Wuhrer, et al. “Glycosylation Changes as Important Factors for the Susceptibility to Urinary Tract Infection.” BIOCHEMICAL SOCIETY TRANSACTIONS 39.1 (2011): 349–354. Print.