FimH Adhesin's Binding to E. coli and Its Role in Urinary Tract Infections
Author Information
Author(s): Julie Bouckaert, Jenny Mackenzie, José L de Paz, Beatrice Chipwaza, Devapriya Choudhury, Anton Zavialov, Karin Mannerstedt, Jennifer Anderson, Denis Piérard, Lode Wyns, Peter H Seeberger, Stefan Oscarson, Henri De Greve, Stefan D Knight
Primary Institution: Vrije Universiteit Brussel
Hypothesis
The study investigates whether FimH variants from different E. coli pathotypes exhibit differences in binding affinities to high-mannose structures.
Conclusion
The carbohydrate expression profile of host tissues and natural inhibitors in urine are more significant determinants of bacterial adhesion than variations in the FimH adhesin.
Supporting Evidence
- FimH variants from different E. coli strains show similar binding affinities for high-mannose structures.
- The Asn135Lys mutation in O157 strains abolishes binding.
- Binding is enhanced by specific glycosidic linkages in oligosaccharides.
Takeaway
This study shows that the way E. coli sticks to the bladder is more about what the bladder has on it than about the differences in the E. coli itself.
Methodology
The study used high-mannose microarrays and surface plasmon resonance to measure binding affinities of FimH to various oligosaccharides.
Limitations
The study does not address the in vivo conditions that may affect FimH binding and bacterial adhesion.
Digital Object Identifier (DOI)
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