| Autor: |
Büttner, Henning, Perbandt, Markus, Kohler, Thomas, Kikhney, Alexey, Wolters, Manuel, Christner, Martin, Heise, Marisol, Wilde, Jérôme, Weißelberg, Samira, Both, Anna, Betzel, Christian, Hammerschmidt, Sven, Svergun, Dmitri, Aepfelbacher, Martin, Rohde, Holger |
| Zdroj: |
mBio; October 2020, Vol. 11 Issue: 5 |
| Abstrakt: |
Staphylococcus epidermidisis a leading pathogen in implant-associated hospital infections. The pathogenesis critically depends on bacterial binding to ECM components, specifically fibronectin (Fn). The cell surface-localized, 1-MDa extracellular matrix binding protein (Embp) is essentially characterized by 10 F- and 40 FG-repeats. These repetitive units, each characterized by two α-helical bundles, organize themselves in a rigid, elongated form. Embp binds preferentially to surface-localized but not soluble Fn, with both F- and FG-repeats being sufficient for Fn binding and resulting bacterial adherence. Binding preferentially involves Fn type III domain, specifically residues of FN12 β-sheets C and F. Both play key role in stabilizing the globular Fn conformation, explaining the necessity of Fn surface immobilization for a subsequent interaction with Embp. In comparison to many other bacterial Fn-binding proteins using the Fn N terminus, Embp employs a previously undescribed mechanism supporting the adhesion of S. epidermidisto surface-immobilized Fn. |
| Databáze: |
Supplemental Index |
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