ArticleCommunications biology2021
Staphylococcus aureus vWF-binding protein triggers a strong interaction between clumping factor A and host vWF.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 19 citations in OpenAlex.
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- Peptidylarginine deiminase 4 and ADAMTS13 activity inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- The Small Protein ScrA Influences Staphylococcus aureus Virulence-Related Processes via the SaeRS System.Microbiology spectrum · 2023Article
- Adhesive Virulence Factors ofACS bio & med chem Au · 2022Article
- Functional analysis of intergenic regulatory regions of genes encoding surface adhesins inBiofilm · 2022Article
- Population distributions of single-cell adhesion parameters during the cell cycle from high-throughput robotic fluidic force microscopy.Scientific reports · 2022Article
- Fibronectin binding protein B binds to loricrin and promotes corneocyte adhesion by Staphylococcus aureus.Nature communications · 2022Article
- Non-Canonical Host Intracellular Niche Links to New Antimicrobial Resistance Mechanism.Pathogens (Basel, Switzerland) · 2022Review
- Staphylococcus aureus iron-regulated surface determinant B (IsdB) protein interacts with von Willebrand factor and promotes adherence to endothelial cells.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
The Staphylococcus aureus cell wall-anchored adhesin ClfA binds to the very large blood circulating protein, von Willebrand factor (vWF) via vWF-binding protein (vWbp), a secreted protein that does not bind the cell wall covalently. Here we perform force spectroscopy studies on living bacteria to unravel the molecular mechanism of this interaction. We discover that the presence of all three binding partners leads to very high binding forces (2000 pN), largely outperforming other known ternary complexes involving adhesins. Strikingly, our experiments indicate that a direct interaction involving features of the dock, lock and latch mechanism must occur between ClfA and vWF to sustain the extreme tensile strength of the ternary complex. Our results support a previously undescribed mechanism whereby vWbp activates a direct, ultra-strong interaction between ClfA and vWF. This intriguing interaction represents a potential target for therapeutic interventions, including synthetic peptides inhibiting the ultra-strong interactions between ClfA and its ligands.
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