ArticlePLoS biology2011
The bacterial fimbrial tip acts as a mechanical force sensor.
Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 86 citations in OpenAlex.
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- A novel post-translational modification of fimbriae drives pathogenicity inbioRxiv : the preprint server for biology · 2025Article
- Chain formation mediated by Escherichia coli immunoglobulin-binding proteins EibD and EibG depends on expression levels and localization of proteins.Scientific reports · 2025Article
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- Emerging Approaches for Mitigating Biofilm-Formation-Associated Infections in Farm, Wild, and Companion Animals.Pathogens (Basel, Switzerland) · 2024Review
- Rate limiting step of the allosteric activation of the bacterial adhesin FimH investigated by molecular dynamics simulations.Proteins · 2024Article
- Screening of antigenic epitopes related to the adhesion of the avian Escherichia coli Type 1 Fimbrial Agglutinin Domain.BMC veterinary research · 2023Article
- Effect of Gravity on Bacterial Adhesion to Heterogeneous Surfaces.Pathogens (Basel, Switzerland) · 2023Article
- Binding site plasticity regulation of the FimH catch-bond mechanism.Biophysical journal · 2023Article
- Recombinant FimH Adhesin Demonstrates How the Allosteric Catch Bond Mechanism Can Support Fast and Strong Bacterial Attachment in the Absence of Shear.Journal of molecular biology · 2022Article
- Adhesion of Enteropathogenic, Enterotoxigenic, and Commensal Escherichia coli to the Major Zymogen Granule Membrane Glycoprotein 2.Applied and environmental microbiology · 2022Article
- Conserved FimH mutations in the globalComputational and structural biotechnology journal · 2022Article
- Anisotropy in mechanical unfolding of protein upon partner-assisted pulling and handle-assisted pulling.Communications biology · 2021Article
- Conformational stability of the bacterial adhesin, FimH, with an inactivating mutation.Proteins · 2021Article
- Bactericidal efficiency of micro- and nanostructured surfaces: a critical perspective.RSC advances · 2021Review
- Poloxamer 338 Affects Cell Adhesion and Biofilm Formation inPathogens (Basel, Switzerland) · 2020Article
- RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain.Proteins · 2020Article
- Urinary tract infections: microbial pathogenesis, host-pathogen interactions and new treatment strategies.Nature reviews. Microbiology · 2020Review
- A shear stress micromodel of urinary tract infection by the Escherichia coli producing Dr adhesin.PLoS pathogens · 2020Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
There is increasing evidence that the catch bond mechanism, where binding becomes stronger under tensile force, is a common property among non-covalent interactions between biological molecules that are exposed to mechanical force in vivo. Here, by using the multi-protein tip complex of the mannose-binding type 1 fimbriae of Escherichia coli, we show how the entire quaternary structure of the adhesive organella is adapted to facilitate binding under mechanically dynamic conditions induced by flow. The fimbrial tip mediates shear-dependent adhesion of bacteria to uroepithelial cells and demonstrates force-enhanced interaction with mannose in single molecule force spectroscopy experiments. The mannose-binding, lectin domain of the apex-positioned adhesive protein FimH is docked to the anchoring pilin domain in a distinct hooked manner. The hooked conformation is highly stable in molecular dynamics simulations under no force conditions but permits an easy separation of the domains upon application of an external tensile force, allowing the lectin domain to switch from a low- to a high-affinity state. The conformation between the FimH pilin domain and the following FimG subunit of the tip is open and stable even when tensile force is applied, providing an extended lever arm for the hook unhinging under shear. Finally, the conformation between FimG and FimF subunits is highly flexible even in the absence of tensile force, conferring to the FimH adhesin an exploratory function and high binding rates. The fimbrial tip of type 1 Escherichia coli is optimized to have a dual functionality: flexible exploration and force sensing. Comparison to other structures suggests that this property is common in unrelated bacterial and eukaryotic adhesive complexes that must function in dynamic conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.