Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus

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 similar to1.1-MDa protein in S. aureus, termed Ebb (for ECM-binding protein homologue), which has homology to other ECM-binding proteins. Ebb 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 Ebb was cloned, overexpressed, and used in ligand-binding studies to determine Ebb 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 Ebb to be cell envelope associated and is proposed to form a specialized surface structure involved in cellular adhesion.