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Cited by 447

The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.

Receptor binding studies disclose a novel class of high‐affinity inhibitors of the Escherichia coli FimH adhesin

Open access
Bouckaert, Julie, Berglund, Jenny, Schembri, Mark, De Genst, Erwin, Cools, Lieve, Wuhrer, Manfred, Hung, Chia‐Suei, Pinkner, Jerome, Slättegård, Rikard, Zavialov, Anton, Choudhury, Devapriya, Langermann, Solomon, Hultgren, Scott J., Wyns, Lode, Klemm, Per, Oscarson, Stefan, Knight, Stefan D., De Greve, Henri·2005·Molecular Microbiology
DOI 10.1111/j.1365-2958.2004.04415.x
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Abstract

Summary: Mannose‐binding type 1 pili are important virulence factors for the establishment of Escherichia coli urinary tract infections (UTIs). These infections are initiated by adhesion of uropathogenic E. coli to uroplakin receptors in the uroepithelium via the FimH adhesin located at the tips of type 1 pili. Blocking of bacterial adhesion is able to prevent infection. Here, we provide for the first time binding data of the molecular events underlying type 1 fimbrial adherence, by crystallographic analyses of the FimH receptor binding domains from a uropathogenic and a K‐12 strain, and affinity measurements with mannose, common mono‐ and disaccharides, and a series of alkyl and aryl mannosides. Our results illustrate that the lectin domain of the FimH adhesin is a stable and functional entity and that an exogenous butyl α‐ d‐mannoside, bound in the crystal structures, exhibits a significantly better affinity for FimH (K d = 0.15 µM) than mannose (K d = 2.3 µM). Exploration of the binding affinities of α‐ d‐mannosides with longer alkyl tails revealed affinities up to 5 nM. Aryl mannosides and fructose can also bind with high affinities to the FimH lectin domain, with a 100‐fold improvement and 15‐fold reduction in affinity, respectively, compared with mannose. Taken together, these relative FimH affinities correlate exceptionally well with the relative concentrations of the same glycans needed for the inhibition of adherence of type 1 piliated E. coli. We foresee that our findings will spark new ideas and initiatives for the development of UTI vaccines and anti‐adhesive drugs to prevent anticipated and recurrent UTIs.

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Crossref · 10.1111/j.1365-2958.2004.04415.x

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Metadata

Authors
Bouckaert, J., Berglund, J., Schembri, M., De Genst, E., Cools, L., Wuhrer, M., Hung, C., Pinkner, J., Slättegård, R., Zavialov, A., Choudhury, D., Langermann, S., Hultgren, S. J., Wyns, L., Klemm, P., Oscarson, S., Knight, S. D., & De Greve, H.
Venue
Molecular Microbiology
Publisher
Wiley
Published
2004-11-25
Volume
55
Issue
2
Pages
441-455
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
DOI
10.1111/j.1365-2958.2004.04415.x
OpenAlex
W2137344636
Cited by
447
References
69
FWCI
4.59
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Receptor binding studies disclose a novel class of high‐affinity inhibitors of the Escherichia coli FimH adhesin. https://app.cochat.ai/papers/10.1111/j.1365-2958.2004.04415.x
The paper
Bouckaert, J., Berglund, J., Schembri, M., De Genst, E., Cools, L., Wuhrer, M., Hung, C., Pinkner, J., Slättegård, R., Zavialov, A., Choudhury, D., Langermann, S., Hultgren, S. J., Wyns, L., Klemm, P., Oscarson, S., Knight, S. D., & De Greve, H. (2005). Receptor binding studies disclose a novel class of high‐affinity inhibitors of the Escherichia coli FimH adhesin. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.2004.04415.x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.