ArticleThe Journal of biological chemistry2016
Molecular Interactions of Human Plasminogen with Fibronectin-binding Protein B (FnBPB), a Fibrinogen/Fibronectin-binding Protein from Staphylococcus aureus.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 58 citations in OpenAlex.
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- The role of human extracellular matrix proteins in defining Staphylococcus aureus biofilm infections.FEMS microbiology reviews · 2024Review
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- von Willebrand factor-binding protein (vWbp)-activated factor XIII and transglutaminase 2 (TG2) promote cross-linking between FnBPA from Staphylococcus aureus and fibrinogen.Scientific reports · 2023Article
- The Recruitment and Activation of Plasminogen by Bacteria-The Involvement in Chronic Infection Development.International journal of molecular sciences · 2023Review
- The A domain of clonal complex 1-type fibronectin binding protein B promotes adherence and biofilm formation inMicrobiology (Reading, England) · 2023Article
- Interaction of theACS nanoscience Au · 2023Article
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- A genetic regulatory see-saw of biofilm and virulence in MRSA pathogenesis.Frontiers in microbiology · 2023Review
- Adhesive Virulence Factors ofACS bio & med chem Au · 2022Article
- Diversity and pathogenesis of Staphylococcus aureus from bovine mastitis: current understanding and future perspectives.BMC veterinary research · 2022Review
- Monoclonal Antibodies Targeting Surface-Exposed and Secreted Proteins from Staphylococci.Vaccines · 2021Review
- An overview of moonlighting proteins in Staphylococcus aureus infection.Archives of microbiology · 2021Review
- Epitope-specific immunity against Staphylococcus aureus coproporphyrinogen III oxidase.NPJ vaccines · 2021Article
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- The Recombinant Expression Proteins FnBP and ClfA FromFrontiers in veterinary science · 2021Article
- Binding of Plasminogen toFrontiers in microbiology · 2021Article
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
Staphylococcus aureus is a commensal bacterium that has the ability to cause superficial and deep-seated infections. Like several other invasive pathogens, S. aureus can capture plasminogen from the human host where it can be converted to plasmin by host plasminogen activators or by endogenously expressed staphylokinase. This study demonstrates that sortase-anchored cell wall-associated proteins are responsible for capturing the bulk of bound plasminogen. Two cell wall-associated proteins, the fibrinogen- and fibronectin-binding proteins A and B, were found to bind plasminogen, and one of them, FnBPB, was studied in detail. Plasminogen captured on the surface of S. aureus- or Lactococcus lactis-expressing FnBPB could be activated to the potent serine protease plasmin by staphylokinase and tissue plasminogen activator. Plasminogen bound to recombinant FnBPB with a KD of 0.532 μm as determined by surface plasmon resonance. Plasminogen binding did not to occur by the same mechanism through which FnBPB binds to fibrinogen. Indeed, FnBPB could bind both ligands simultaneously indicating that their binding sites do not overlap. The N3 subdomain of FnBPB contains the full plasminogen-binding site, and this includes, at least in part, two conserved patches of surface-located lysine residues that were recognized by kringle 4 of the host protein.
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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.