ArticleThe Journal of biological chemistry2008
FimH forms catch bonds that are enhanced by mechanical force due to allosteric regulation.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
121 citing papers in PubMed, 217 citations in OpenAlex.
- Pharmacologic glycoengineering of Fcγ receptor IIIa enhances force-resistant IgG-FcγR interactions and anti-tumor antibody efficacy.Immunity · 2026Article
- Massively parallel bead-free force spectroscopy with fluorescence.Science advances · 2026Article
- Review
- Effects of fluid shear stress on oral biofilm formation and composition and the transcriptional response of Streptococcus gordonii.Molecular oral microbiology · 2024Article
- Engineering tunable catch bonds with DNA.Nature communications · 2024Article
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- A flow cytometry method for quantitative measurement and molecular investigation of the adhesion of bacteria to yeast cells.Scientific reports · 2024Article
- Engineering an artificial catch bond using mechanical anisotropy.Nature communications · 2024Article
- Rate limiting step of the allosteric activation of the bacterial adhesin FimH investigated by molecular dynamics simulations.Proteins · 2024Article
- Shear force enhances adhesion ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Antioxidant, Volatile Compounds; Antimicrobial, Anti-Inflammatory, and Dermatoprotective Properties ofMolecules (Basel, Switzerland) · 2023Article
- Binding site plasticity regulation of the FimH catch-bond mechanism.Biophysical journal · 2023Article
- Periodically disturbing biofilms reduces expression of quorum sensing-regulated virulence factors iniScience · 2023Article
- Shear force enhances adhesion ofbioRxiv : the preprint server for biology · 2023Article
- Catch bond models may explain how force amplifies TCR signaling and antigen discrimination.Nature communications · 2023Article
- Bacteria in Fluid Flow.Journal of bacteriology · 2023Review
- High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion.Communications biology · 2023Article
- Disturbing the Spatial Organization of Biofilm Communities Affects Expression ofApplied and environmental microbiology · 2023Article
- Phenotypic Assessment of Clinical Escherichia coli Isolates as an Indicator for Uropathogenic Potential.mSystems · 2022Article
- Review
61 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The bacterial adhesive protein, FimH, is the most common adhesin of Escherichia coli and mediates weak adhesion at low flow but strong adhesion at high flow. There is evidence that this occurs because FimH forms catch bonds, defined as bonds that are strengthened by tensile mechanical force. Here, we applied force to single isolated FimH bonds with an atomic force microscope in order to test this directly. If force was loaded slowly, most of the bonds broke up at low force (<60 piconewtons of rupture force). However, when force was loaded rapidly, all bonds survived until much higher force (140-180 piconewtons of rupture force), behavior that indicates a catch bond. Structural mutations or pretreatment with a monoclonal antibody, both of which allosterically stabilize a high affinity conformation of FimH, cause all bonds to survive until high forces regardless of the rate at which force is applied. Pretreatment of FimH bonds with intermediate force has the same strengthening effect on the bonds. This demonstrates that FimH forms catch bonds and that tensile force induces an allosteric switch to the high affinity, strong binding conformation of the adhesin. The catch bond behavior of FimH, the amount of force needed to regulate FimH, and the allosteric mechanism all provide insight into how bacteria bind and form biofilms in fluid flow. Additionally, these observations may provide a means for designing antiadhesive mechanisms.
Indexed as
Identifiers
What OpenQuestion holds
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.