ArticleCommunications biology2023
High-force catch bonds between the Staphylococcus aureus surface protein SdrE and complement regulator factor H drive immune evasion.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Integrated multi-omics reveals coordinatedmSystems · 2026Article
- Different Cell Wall Compositions of ESKAPE Isolates on Glass Surfaces Impact Adhesion Adaptability to Dynamic Shear Stress.Microorganisms · 2026Article
- Immune evasion of multidrug-resistant bacteria: insights from lung innate immune cells and targeted therapies.Frontiers in cellular and infection microbiology · 2026Review
- Preventive Immunology for Livestock and Zoonotic Infectious Diseases in the One Health Era: From Mechanistic Insights to Innovative Interventions.Veterinary sciences · 2025Review
- Atomic force microscopy at the forefront: unveiling foodborne viruses with biophysical tools.Npj viruses · 2025Review
- Article
- Steamed panax notoginseng mitigates CA-MRSA USA300-induced necroptosis in human neutrophils.Frontiers in pharmacology · 2025Article
- Genome-based model for differentiating between infection and carriageMicrobiology spectrum · 2024Article
- Principles and regulation of mechanosensing.Journal of cell science · 2024Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The invasive bacterial pathogen Staphylococcus aureus recruits the complement regulatory protein factor H (fH) to its surface to evade the human immune system. Here, we report the identification of an extremely high-force catch bond used by the S. aureus surface protein SdrE to efficiently capture fH under mechanical stress. We find that increasing the external force applied to the SdrE-fH complex prolongs the lifetime of the bond at an extraordinary high force, 1,400 pN, above which the bond lifetime decreases as an ordinary slip bond. This catch-bond behavior originates from a variation of the dock, lock and latch interaction, where the SdrE ligand binding domains undergo conformational changes under stress, enabling the formation of long-lived hydrogen bonds with fH. The binding mechanism dissected here represents a potential target for new therapeutics against multidrug-resistant S. aureus strains.
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Registered trials
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