ArticleThe Journal of biological chemistry2018
Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Parallel evolutionary trajectories rewire enteropathogenicGut microbes · 2026Article
- Improving the immunogenicity ofFrontiers in immunology · 2026Article
- Mannose Derivatives as Anti-Infective Agents.International journal of molecular sciences · 2025Review
- Adaptive genetics reveals constraints on protein structure/function by evolving E. coli under constant nutrient limitation.BMC biology · 2025Article
- Structure-based design of an immunogenic, conformationally stabilized FimH antigen for a urinary tract infection vaccine.PLoS pathogens · 2025Article
- An mRNA-based FimH nanoparticle vaccine against uropathogenicFrontiers in immunology · 2025Article
- Cloning and Expression of Pigeon-DerivedGenes · 2024Article
- Screening of antigenic epitopes related to the adhesion of the avian Escherichia coli Type 1 Fimbrial Agglutinin Domain.BMC veterinary research · 2023Article
- Binding site plasticity regulation of the FimH catch-bond mechanism.Biophysical journal · 2023Article
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Article
- 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
- Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin.Journal of molecular biology · 2022Review
- Article
- Conformational stability of the bacterial adhesin, FimH, with an inactivating mutation.Proteins · 2021Article
- FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021Article
- NMR in target driven drug discovery: why not?Journal of biomolecular NMR · 2020Article
- RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain.Proteins · 2020Article
- Cell behavior of the highly sticky bacterium Acinetobacter sp. Tol 5 during adhesion in laminar flows.Scientific reports · 2018Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
For many biological processes such as ligand binding, enzymatic catalysis, or protein folding, allosteric regulation of protein conformation and dynamics is fundamentally important. One example is the bacterial adhesin FimH, where the C-terminal pilin domain exerts negative allosteric control over binding of the N-terminal lectin domain to mannosylated ligands on host cells. When the lectin and pilin domains are separated under shear stress, the FimH-ligand interaction switches in a so-called catch-bond mechanism from the low- to high-affinity state. So far, it has been assumed that the pilin domain is essential for the allosteric propagation within the lectin domain that would otherwise be conformationally rigid. To test this hypothesis, we generated mutants of the isolated FimH lectin domain and characterized their thermodynamic, kinetic, and structural properties using isothermal titration calorimetry, surface plasmon resonance, nuclear magnetic resonance, and X-ray techniques. Intriguingly, some of the mutants mimicked the conformational and kinetic behaviors of the full-length protein and, even in absence of the pilin domain, conducted the cross-talk between allosteric sites and the mannoside-binding pocket. Thus, these mutants represent a minimalistic allosteric system of FimH, useful for further mechanistic studies and antagonist design.
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