ArticleJournal of the American Chemical Society2022
Mechanical Stabilization of a Bacterial Adhesion Complex.
Article in Journal of the American Chemical Society, 2022. 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, 30 citations in OpenAlex.
- High resolution mapping of protein motions in time and space with RMSX and Flipbook.Scientific reports · 2026Article
- Cell Adhesion and Biofilm Development via Force-Sensitive Mechanisms: A Perspective.ACS biomaterials science & engineering · 2026Review
- Propolis Exerts Antibiofilm Activity Against Methicillin-ResistantMicroorganisms · 2025Article
- Micro- and nano-scale adhesion of oral bacteria to biomaterials using atomic force microscopy: A systematic review.The Japanese dental science review · 2025Review
- UltrastrongScience advances · 2025Article
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Article
- De novo DNA-based catch bonds.Nature chemistry · 2024Article
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- Article
- The Force-Dependent Mechanism of an Integrin α4β7-MAdCAM-1 Interaction.International journal of molecular sciences · 2023Article
- Unveiling Mechanical Activation: GAIN Domain Unfolding and Dissociation in Adhesion GPCRs.Nano letters · 2023Article
- Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins.eLife · 2023Article
- High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion.Communications biology · 2023Article
- May the force be with you: The role of hyper-mechanostability of the bone sialoprotein binding protein during early stages ofFrontiers in chemistry · 2023Article
- Protein structure prediction in the era of AI: Challenges and limitations when applying toFrontiers in bioinformatics · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The adhesions between Gram-positive bacteria and their hosts are exposed to varying magnitudes of tensile forces. Here, using an ultrastable magnetic tweezer-based single-molecule approach, we show the catch-bond kinetics of the prototypical adhesion complex of SD-repeat protein G (SdrG) to a peptide from fibrinogen β (Fgβ) over a physiologically important force range from piconewton (pN) to tens of pN, which was not technologically accessible to previous studies. At 37 °C, the lifetime of the complex exponentially increases from seconds at several pN to ∼1000 s as the force reaches 30 pN, leading to mechanical stabilization of the adhesion. The dissociation transition pathway is determined as the unbinding of a critical β-strand peptide ("latch" strand of SdrG that secures the entire adhesion complex) away from its binding cleft, leading to the dissociation of the Fgβ ligand. Similar mechanical stabilization behavior is also observed in several homologous adhesions, suggesting the generality of catch-bond kinetics in such bacterial adhesions. We reason that such mechanical stabilization confers multiple advantages in the pathogenesis and adaptation of bacteria.
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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.