ArticleBiophysical journal2006
Catch-bond model derived from allostery explains force-activated bacterial adhesion.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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Who cites it
98 citing papers in PubMed.
- Reversible formation of von-Willebrand-factor-platelet aggregates in microvascular blood flow.PNAS nexus · 2025Article
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination.Nature communications · 2025Article
- A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- De novo DNA-based catch bonds.Nature chemistry · 2024Article
- Engineering tunable catch bonds with DNA.Nature communications · 2024Article
- Microbiology of human spaceflight: microbial responses to mechanical forces that impact health and habitat sustainability.Microbiology and molecular biology reviews : MMBR · 2024Review
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- Emergence of slip-ideal-slip behavior in tip-links serve as force filters of sound in hearing.Nature communications · 2024Article
- Topology of molecular deformations induces triphasic catch bonding in selectin-ligand bonds.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Can a bulky glycocalyx promote catch bonding in early integrin adhesion? Perhaps a bit.Biomechanics and modeling in mechanobiology · 2024Article
- Cardiac desmosomal adhesion relies on ideal-, slip- and catch bonds.Scientific reports · 2024Article
- Molecular mechanisms of catch bonds and their implications for platelet hemostasis.Biophysical reviews · 2023Review
- The Energetic Landscape of Catch Bonds in TCR Interfaces.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Binding site plasticity regulation of the FimH catch-bond mechanism.Biophysical journal · 2023Article
- High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion.Communications biology · 2023Article
- Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments.Communications biology · 2023Article
- Can a bulky glycocalyx promote catch bonding in early integrin adhesion? Perhaps a bit.bioRxiv : the preprint server for biology · 2023Article
- Multi-level Force-dependent Allosteric Enhancement of αE-catenin Binding to F-actin by Vinculin.Journal of molecular biology · 2023Article
- Review
38 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
High shear enhances the adhesion of Escherichia coli bacteria binding to mannose coated surfaces via the adhesin FimH, raising the question as to whether FimH forms catch bonds that are stronger under tensile mechanical force. Here, we study the length of time that E. coli pause on mannosylated surfaces and report a double exponential decay in the duration of the pauses. This double exponential decay is unlike previous single molecule or whole cell data for other catch bonds, and indicates the existence of two distinct conformational states. We present a mathematical model, derived from the common notion of chemical allostery, which describes the lifetime of a catch bond in which mechanical force regulates the transitions between two conformational states that have different unbinding rates. The model explains these characteristics of the data: a double exponential decay, an increase in both the likelihood and lifetime of the high-binding state with shear stress, and a biphasic effect of force on detachment rates. The model parameters estimated from the data are consistent with the force-induced structural changes shown earlier in FimH. This strongly suggests that FimH forms allosteric catch bonds. The model advances our understanding of both catch bonds and the role of allostery in regulating protein activity.
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