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The giant Staphylococcus epidermidis surface protein Embp binds selectively to fibrillated fibronectin through a Velcro-like mechanism

Staphylococcus epidermidis is a major cause of implant-associated infections. It attaches to implants via adsorbed host proteins, and one prominent adhesin is the fibronectin-binding protein Embp. This study aims to determine how S. epidermidis can attach to surfaces via adsorbed fibronectin, when fibronectin is also abundant in solution. We hypothesize that Embp interacts selectively with adsorbed fibronectin if adsorption introduces a conformational change. We produced a model system in which Fn adsorbed in either globular or fibrillated conformation. Embp-mediated attachment occurred exclusively to fibrillated Fn, and involved subdomain F3 12th-14th, which is buried in globular Fn. Single-molecule force spectroscopy revealed a Velcro-like interaction, as a single of the 60 Fn-binding repeats interacted weakly, while 15 FG-repeats attached strongly with the fibrillated ligand. This mechanism enables selective and strong attachment to immobilized Fn via a single surface protein: a mechanism that proved particularly beneficial for attachment under high flow conditions.