ArticleNature communications2016
Catch-bond mechanism of the bacterial adhesin FimH.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.
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Who cites it
138 citing papers in PubMed, 231 citations in OpenAlex.
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- Biophysical and functional characterization of the Escherichia coli Dr fimbrial envelope reveals its importance for pathogenesis and lithogenesis.PLoS pathogens · 2026Article
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- RstAB activates type 1 fimbriae to promote uropathogeniciScience · 2026Article
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- PVC microplastics facilitate uropathogenic Escherichia coli pathogenicity by enhancing host cell invasion and mitochondrial-dependent pyroptosis.Nature communications · 2026Article
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- Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- HMGB1 functions as a critical mediator of host defense at the gut mucosal barrier.Cell host & microbe · 2026Article
- Cell Adhesion and Biofilm Development via Force-Sensitive Mechanisms: A Perspective.ACS biomaterials science & engineering · 2026Review
- Decoding epithelial-immune cell crosstalk in uropathogenicFrontiers in microbiology · 2026Review
- Computational Analysis of Periplasmic Protein-Mediated Resistance to Membrane Extraction of a Trimeric Autotransporter Adhesin Transmembrane Domain.Computational and structural biotechnology journal · 2026Article
- Harnessing pro-inflammatory and immunopathologic immune responses in urinary tract infections for vaccine development: it's all about a balance.Frontiers in immunology · 2026Review
- Infective endocarditis caused byThe Journal of international medical research · 2025Article
- Antibodies disrupt bacterial adhesion by ligand mimicry and allosteric interference.Nature communications · 2025Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Beyond FimH: Diversity and Relevance of Carbohydrate-Binding Fimbrial Proteins in Escherichia coli.Chembiochem : a European journal of chemical biology · 2025Review
78 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ligand-receptor interactions that are reinforced by mechanical stress, so-called catch-bonds, play a major role in cell-cell adhesion. They critically contribute to widespread urinary tract infections by pathogenic Escherichia coli strains. These pathogens attach to host epithelia via the adhesin FimH, a two-domain protein at the tip of type I pili recognizing terminal mannoses on epithelial glycoproteins. Here we establish peptide-complemented FimH as a model system for fimbrial FimH function. We reveal a three-state mechanism of FimH catch-bond formation based on crystal structures of all states, kinetic analysis of ligand interaction and molecular dynamics simulations. In the absence of tensile force, the FimH pilin domain allosterically accelerates spontaneous ligand dissociation from the FimH lectin domain by 100,000-fold, resulting in weak affinity. Separation of the FimH domains under stress abolishes allosteric interplay and increases the affinity of the lectin domain. Cell tracking demonstrates that rapid ligand dissociation from FimH supports motility of piliated E. coli on mannosylated surfaces in the absence of shear force.
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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.