ArticleThe Journal of experimental medicine2005
Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis.
Article in The Journal of experimental medicine, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
128 citing papers in PubMed, 1 synthesis or guideline pooled it, 284 citations in OpenAlex.
- Host-Bacterium Interaction Mechanisms inInternational journal of molecular sciences · 2023Pooled it
- Combinatorial phenotypic signatures distinguish persistent from resolving methicillin-resistant Staphylococcus aureus bacteremia isolates.Antimicrobial agents and chemotherapy · 2011Trial
- Genomic, proteolytic, and phenotypic characterization ofMicrobiology spectrum · 2026Article
- Genetic determinants of Staphylococcus aureus adhesion shape virulence trade-offs in bacteremia.Nature communications · 2026Article
- Discovery of a new fibronectin-binding surface protein ofFrontiers in cellular and infection microbiology · 2026Article
- Molecular investigation of biofilm-forming genes in staphylococci isolated from dogs in Ilam, Iran.Veterinary research forum : an international quarterly journal · 2026Article
- Dual transcriptomic profiling ofmBio · 2025Article
- Prophage-encoded methyltransferase drives adaptation of community-acquired methicillin-resistant Staphylococcus aureus.The Journal of clinical investigation · 2025Article
- A Novel Interaction of Staphylococcal Protein A With Human Fibronectin and Its Implications in Host Cell Adhesion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Review
- The Evolving Landscape of Infective Endocarditis: Difficult-to-Treat Resistance Bacteria and Novel Diagnostics at the Foreground.Journal of clinical medicine · 2025Review
- A natural killer cell mimic against intracellular pathogen infections.Science advances · 2024Article
- Article
- New Thiosemicarbazide Derivatives with Multidirectional Biological Action.Molecules (Basel, Switzerland) · 2024Article
- Review
- Protein Disulfide Isomerase and Extracellular Adherence Protein Cooperatively Potentiate Staphylococcal Invasion into Endothelial Cells.Microbiology spectrum · 2023Article
- Bacteria in Fluid Flow.Journal of bacteriology · 2023Review
- Functional diversity of staphylococcal surface proteins at the host-microbe interface.Frontiers in microbiology · 2023Review
- Innovations in Evaluating Statin Benefit and Efficacy inInternational journal of molecular sciences · 2022Review
- Activation of Human Platelets byPathogens (Basel, Switzerland) · 2022Article
68 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The expression of Staphylococcus aureus adhesins in Lactococcus lactis identified clumping factor A (ClfA) and fibronectin-binding protein A (FnBPA) as critical for valve colonization in rats with experimental endocarditis. This study further analyzed their role in disease evolution. Infected animals were followed for 3 d. ClfA-positive lactococci successfully colonized damaged valves, but were spontaneously eradicated over 48 h. In contrast, FnBPA-positive lactococci progressively increased bacterial titers in vegetations and spleens. At imaging, ClfA-positive lactococci were restricted to the vegetations, whereas FnBPA-positive lactococci also invaded the adjacent endothelium. This reflected the capacity of FnBPA to trigger cell internalization in vitro. Because FnBPA carries both fibrinogen- and fibronectin-binding domains, we tested the role of these functionalities by deleting the fibrinogen-binding domain of FnBPA and supplementing it with the fibrinogen-binding domain of ClfA in cis or in trans. Deletion of the fibrinogen-binding domain of FnBPA did not alter fibronectin binding and cell internalization in vitro. However, it totally abrogated valve infectivity in vivo. This ability was restored in cis by inserting the fibrinogen-binding domain of ClfA into truncated FnBPA, and in trans by coexpressing full-length ClfA and truncated FnBPA on two separate plasmids. Thus, fibrinogen and fibronectin binding could cooperate for S. aureus valve colonization and endothelial invasion in vivo.
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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.