ArticleNature communications2020
Force-clamp spectroscopy identifies a catch bond mechanism in a Gram-positive pathogen.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 47 citations in OpenAlex.
- Review
- Massively parallel bead-free force spectroscopy with fluorescence.Science advances · 2026Article
- Different Cell Wall Compositions of ESKAPE Isolates on Glass Surfaces Impact Adhesion Adaptability to Dynamic Shear Stress.Microorganisms · 2026Article
- Bacterial species with different nanocolony morphologies have distinct flow-dependent colonization behaviors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024Article
- Engineering an artificial catch bond using mechanical anisotropy.Nature communications · 2024Article
- High-throughput virtual search of small molecules for controlling the mechanical stability of human CD4.The Journal of biological chemistry · 2024Article
- Shear force enhances adhesion ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Energetic Landscape of Catch Bonds in TCR Interfaces.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Shear force enhances adhesion ofbioRxiv : the preprint server for biology · 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
- Interaction of theACS nanoscience Au · 2023Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Mechanical Stabilization of a Bacterial Adhesion Complex.Journal of the American Chemical Society · 2022Article
- 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
- Optimal Sacrificial Domains in Mechanical Polyproteins:JACS Au · 2022Article
- The Power of Touch: Type 4 Pili, the von Willebrand A Domain, and Surface Sensing by Pseudomonas aeruginosa.Journal of bacteriology · 2022Review
- Transmission of Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Physical forces have profound effects on cellular behavior, physiology, and disease. Perhaps the most intruiguing and fascinating example is the formation of catch-bonds that strengthen cellular adhesion under shear stresses. Today mannose-binding by the Escherichia coli FimH adhesin remains one of the rare microbial catch-bond thoroughly characterized at the molecular level. Here we provide a quantitative demonstration of a catch-bond in living Gram-positive pathogens using force-clamp spectroscopy. We show that the dock, lock, and latch interaction between staphylococcal surface protein SpsD and fibrinogen is strong, and exhibits an unusual catch-slip transition. The bond lifetime first grows with force, but ultimately decreases to behave as a slip bond beyond a critical force (~1 nN) that is orders of magnitude higher than for previously investigated complexes. This catch-bond, never reported for a staphylococcal adhesin, provides the pathogen with a mechanism to tightly control its adhesive function during colonization and infection.
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.