The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Tamm-Horsfall Protein Binds to Type 1 Fimbriated Escherichia coli and Prevents E. coli from Binding to Uroplakin Ia and Ib Receptors
Open accessAbstract
The adherence of uropathogenic Escherichia coli to the urothelial surface, a critical first step in the pathogenesis of urinary tract infection (UTI), is controlled by three key elements: E. coli adhesins, host receptors, and host defense mechanisms. Although much has been learned about E. coli adhesins and their urothelial receptors, little is known about the role of host defense in the adherence process. Here we show that Tamm-Horsfall protein (THP) is the principal urinary protein that binds specifically to type 1 fimbriated E. coli, the main cause of UTI. The binding was highly specific and saturable and could be inhibited by d-mannose and abolished by endoglycosidase H treatment of THP, suggesting that the binding is mediated by the high-mannose moieties of THP. It is species-conserved, occurring in both human and mouse THPs. In addition, the binding to THP was much greater with an E. coli strain bearing a phenotypic variant of the type 1 fimbrial FimH adhesin characteristic of those prevalent in UTI isolates compared with the one prevalent in isolates from the large intestine of healthy individuals. Finally, a physiological concentration of THP completely abolished the binding of type 1 fimbriated E. coli to uroplakins Ia and Ib, two putative urothelial receptors for type 1 fimbriae. These results establish, on a functional level, that THP contains conserved high-mannose moieties capable of specific interaction with type 1 fimbriae and strongly suggest that this major urinary glycoprotein is a key urinary anti-adherence factor serving to prevent type 1 fimbriated E. coli from binding to the urothelial receptors.
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Cites
Induction and Evasion of Host Defenses by Type 1-Piliated Uropathogenic Escherichia coli
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Cited by
Microfold (M) cells: important immunosurveillance posts in the intestinal epithelium
Mabbott, N. A., Donaldson, D. S., Ohno, H., Williams, I. R., & Mahajan, A. (2013) · Mucosal Immunology · doi:10.1038/mi.2013.30 · Cited by 721
“coli and may function to prevent these bacteria from binding to uroepithelial cells.(46) Although the expression of Umod by Peyer’s patch M cells is much lower than Gp2, their similar characteristics imply that each protein may aid the sampling of FimHþ bacteria in the gut lumen.”
BackgroundAnti-adhesion therapy of bacterial diseases: prospects and problems
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Self-citationStructural basis of tropism of Escherichia coli to the bladder during urinary tract infection
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Tamm-Horsfall glycoprotein: biology and clinical relevance
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Systemic multicompartmental effects of the gut microbiome on mouse metabolic phenotypes
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Metadata
- Authors
- Pak, J., Pu, Y., Zhang, Z.-T., Hasty, D. L., & Wu, X.-R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 276
- Issue
- 13
- Pages
- 9924-9930
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2022548242
- Cited by
- 290
- References
- 34
- FWCI
- 5.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Pak, J., Pu, Y., Zhang, Z.-T., Hasty, D. L., & Wu, X.-R. (2001). Tamm-Horsfall Protein Binds to Type 1 Fimbriated Escherichia coli and Prevents E. coli from Binding to Uroplakin Ia and Ib Receptors. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m008610200
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