Adhesion of Escherichia coli under flow conditions reveals potential novel effects of FimH mutations View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-03

AUTHORS

T. Feenstra, M. S. Thøgersen, E. Wieser, A. Peschel, M. J. Ball, R. Brandes, S. C. Satchell, T. Stockner, F. M. Aarestrup, A. J. Rees, R. Kain

ABSTRACT

FimH-mediated adhesion of Escherichia coli to bladder epithelium is a prerequisite for urinary tract infections. FimH is also essential for blood-borne bacterial dissemination, but the mechanisms are poorly understood. The purpose of this study was to assess the influence of different FimH mutations on bacterial adhesion using a novel adhesion assay, which models the physiological flow conditions bacteria are exposed to. We introduced 12 different point mutations in the mannose binding pocket of FimH in an E. coli strain expressing type 1 fimbriae only (MSC95-FimH). We compared the bacterial adhesion of each mutant across several commonly used adhesion assays, including agglutination of yeast, adhesion to mono- and tri-mannosylated substrates, and static adhesion to bladder epithelial and endothelial cells. We performed a comparison of these assays to a novel method that we developed to study bacterial adhesion to mammalian cells under flow conditions. We showed that E. coli MSC95-FimH adheres more efficiently to microvascular endothelium than to bladder epithelium, and that only endothelium supports adhesion at physiological shear stress. The results confirmed that mannose binding pocket mutations abrogated adhesion. We demonstrated that FimH residues E50 and T53 are crucial for adhesion under flow conditions. The coating of endothelial cells on biochips and modelling of physiological flow conditions enabled us to identify FimH residues crucial for adhesion. These results provide novel insights into screening methods to determine the effect of FimH mutants and potentially FimH antagonists. More... »

PAGES

467-478

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10096-016-2820-8

DOI

http://dx.doi.org/10.1007/s10096-016-2820-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017529018

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27816993


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