ArticleInfection and immunity2002
Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus.
Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 131 citations in OpenAlex.
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- Staphylococcus aureus genotype variation among and within periprosthetic joint infections.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2022Article
- Antibiotic Resistance and Pathogenomics ofMicroorganisms · 2021Article
- Comparative Transcriptomic Analysis of Staphylococcus aureus Associated with Periprosthetic Joint Infection under in Vivo and in Vitro Conditions.The Journal of molecular diagnostics : JMD · 2021Article
- Biofilms by bacterial human pathogens: Clinical relevance - development, composition and regulation - therapeutical strategies.Microbial cell (Graz, Austria) · 2021Review
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- Anti-MRSA agent discovery using Caenorhabditis elegans-based high-throughput screening.Journal of microbiology (Seoul, Korea) · 2020Review
- Review
- Staphylococcus aureus adhesion in endovascular infections is controlled by the ArlRS-MgrA signaling cascade.PLoS pathogens · 2019Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order for Staphylococcus aureus to adhere to host extracellular matrix (ECM) substrates, it elicits a wide range of surface proteins. We have characterized a novel approximately 1.1-MDa protein in S. aureus, termed Ebh (for ECM-binding protein homologue), which has homology to other ECM-binding proteins. Ebh consists of several domains, including a large central region with 44 imperfect repeats of 126 amino acids. Expression analysis revealed ebh to be growth phase regulated and repressed by agr. A fragment of the central repeat region of Ebh was cloned, overexpressed, and used in ligand-binding studies to determine Ebh function. The recombinant protein was found to specifically bind human fibronectin. Ebh is produced during human infection since serum samples taken from patients with confirmed S. aureus infections were found to contain anti-Ebh antibodies. Localization studies revealed Ebh to be cell envelope associated and is proposed to form a specialized surface structure involved in cellular adhesion.
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