ArticleThe Journal of biological chemistry2012
Dissociation rate constants of human fibronectin binding to fibronectin-binding proteins on living Staphylococcus aureus isolated from clinical patients.
Article in The Journal of biological chemistry, 2012. 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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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.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Cell Adhesion and Biofilm Development via Force-Sensitive Mechanisms: A Perspective.ACS biomaterials science & engineering · 2026Review
- Functional analysis of intergenic regulatory regions of genes encoding surface adhesins inBiofilm · 2022Article
- The biophysics of bacterial infections: Adhesion events in the light of force spectroscopy.Cell surface (Amsterdam, Netherlands) · 2021Article
- Host blood proteins as bridging ligand in bacterial aggregation as well as anchor point for adhesion in the molecular pathogenesis of Staphylococcus aureus infections.Micron (Oxford, England : 1993) · 2021Article
- How Microbes Use Force To Control Adhesion.Journal of bacteriology · 2020Review
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- The Multivalent Role of Fibronectin-Binding Proteins A and B (FnBPA and FnBPB) ofFrontiers in microbiology · 2020Review
- Binding Strength of Gram-Positive Bacterial Adhesins.Frontiers in microbiology · 2020Review
- Distinct Binding Interactions of αBiophysical journal · 2019Article
- Fibrinogen binding is affected by amino acid substitutions in C-terminal repeat region of fibronectin binding protein A.Scientific reports · 2019Article
- Amino acid polymorphisms in the fibronectin-binding repeats of fibronectin-binding protein A affect bond strength and fibronectin conformation.The Journal of biological chemistry · 2017Article
- Curli mediate bacterial adhesion to fibronectin via tensile multiple bonds.Scientific reports · 2016Article
- Zinc-dependent mechanical properties of Staphylococcus aureus biofilm-forming surface protein SasG.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Stuck in the Middle: Fibronectin-Binding Proteins in Gram-Positive Bacteria.Frontiers in microbiology · 2016Review
- Endovascular infections caused by methicillin-resistant Staphylococcus aureus are linked to clonal complex-specific alterations in binding and invasion domains of fibronectin-binding protein A as well as the occurrence of fnbB.Infection and immunity · 2015Article
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- saeRS and sarA act synergistically to repress protease production and promote biofilm formation in Staphylococcus aureus.PloS one · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Staphylococcus aureus is part of the indigenous microbiota of humans. Sometimes, S. aureus bacteria enter the bloodstream, where they form infections on implanted cardiovascular devices. A critical, first step in such infections is a bond that forms between fibronectin-binding protein (FnBP) on S. aureus and host proteins, such as fibronectin (Fn), that coat the surface of implants in vivo. In this study, native FnBPs on living S. aureus were shown to form a mechanically strong conformational structure with Fn by atomic force microscopy. The tensile acuity of this bond was probed for 46 bloodstream isolates, each from a patient with a cardiovascular implant. By analyzing the force spectra with the worm-like chain model, we determined that the binding events were consistent with a multivalent, cluster bond consisting of ~10 or ~80 proteins in parallel. The dissociation rate constant (k(off), s(-1)) of each multibond complex was determined by measuring strength as a function of the loading rate, normalized by the number of bonds. The bond lifetime (1/k(off)) was two times longer for bloodstream isolates from patients with an infected device (1.79 or 69.47 s for the 10- or 80-bond clusters, respectively; n = 26 isolates) relative to those from patients with an uninfected device (0.96 or 34.02 s; n = 20 isolates). This distinction could not be explained by different amounts of FnBP, as confirmed by Western blots. Rather, amino acid polymorphisms within the Fn-binding repeats of FnBPA explain, at least partially, the statistically (p < 0.05) longer bond lifetime for isolates associated with an infected cardiovascular device.
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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.