ArticleThe Journal of biological chemistry2013
Allosteric coupling in the bacterial adhesive protein FimH.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed.
- Parallel evolutionary trajectories rewire enteropathogenicGut microbes · 2026Article
- Antibodies disrupt bacterial adhesion by ligand mimicry and allosteric interference.Nature communications · 2025Article
- De Novo Design of Miniprotein Inhibitors of Bacterial Adhesins.Research square · 2025Article
- Article
- Orthogonal photoswitching of heterobivalent azobenzene glycoclusters: the effect of glycoligand orientation in bacterial adhesion.Beilstein journal of organic chemistry · 2025Article
- The artificial neural network selects saccharides from natural sources a promise for potential FimH inhibitor to prevent UTI infections.In silico pharmacology · 2024Article
- Rate limiting step of the allosteric activation of the bacterial adhesin FimH investigated by molecular dynamics simulations.Proteins · 2024Article
- 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
- Article
- Conserved FimH mutations in the globalComputational and structural biotechnology journal · 2022Article
- Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core.PLoS pathogens · 2021Article
- 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
- RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain.Proteins · 2020Article
- Targeting Dynamical Binding Processes in the Design of Non-Antibiotic Anti-Adhesives by Molecular Simulation-The Example of FimH.Molecules (Basel, Switzerland) · 2018Review
- Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system.The Journal of biological chemistry · 2018Article
- Rational design strategies for FimH antagonists: new drugs on the horizon for urinary tract infection and Crohn's disease.Expert opinion on drug discovery · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The protein FimH is expressed by the majority of commensal and uropathogenic strains of Escherichia coli on the tips of type 1 fimbriae and mediates adhesion via a catch bond to its ligand mannose. Crystal structures of FimH show an allosteric conformational change, but it remains unclear whether all of the observed structural differences are part of the allosteric mechanism. Here we use the protein structural analysis tool RosettaDesign combined with human insight to identify and synthesize 10 mutations in four regions that we predicted would stabilize one of the conformations of that region. The function of each variant was characterized by measuring binding to the ligand mannose, whereas the allosteric state was determined using a conformation-specific monoclonal antibody. These studies demonstrated that each region investigated was indeed part of the FimH allosteric mechanism. However, the studies strongly suggested that some regions were more tightly coupled to mannose binding and others to antibody binding. In addition, we identified many FimH variants that appear locked in the low affinity state. Knowledge of regulatory sites outside the active and effector sites as well as the ability to make FimH variants locked in the low affinity state may be crucial to the future development of novel antiadhesive and antimicrobial therapies using allosteric regulation to inhibit FimH.
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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.