The anchorless adhesin Eap (extracellular adherence protein) from Staphylococcus aureus selectively recognizes extracellular matrix aggregates but binds promiscuously to monomeric matrix macromolecules

Matrix Biology : Journal of the International Society for Matrix Biology
Uwe HansenPeter Bruckner

Abstract

Besides a number of cell wall-anchored adhesins, the majority of Staphylococcus aureus strains produce anchorless, cell wall-associated proteins, such as Eap (extracellular adherence protein). Eap contains four to six tandem repeat (EAP)-domains. Eap mediates diverse biological functions, including adherence and immunomodulation, thus contributing to S. aureus pathogenesis. Eap binding to host macromolecules is unusually promiscuous and includes matrix or matricellular proteins as well as plasma proteins. The structural basis of this promiscuity is poorly understood. Here, we show that in spite of the preferential location of the binding epitopes within triple helical regions in some collagens there is a striking specificity of Eap binding to different collagen types. Collagen I, but not collagen II, is a binding substrate in monomolecular form. However, collagen I is virtually unrecognized by Eap when incorporated into banded fibrils. By contrast, microfibrils containing collagen VI as well as basement membrane-associated networks containing collagen IV, or aggregates containing fibronectin bound Eap as effectively as the monomeric proteins. Therefore, Eap-binding to extracellular matrix ligands is promiscuous at the molecular...Continue Reading

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Citations

Dec 21, 2007·Journal of Clinical Microbiology·Muzaffar HussainKarsten Becker
Dec 18, 2013·Future Microbiology·Rosanna CoatesMalcolm J Horsburgh
Aug 8, 2007·Trends in Immunology·Triantafyllos ChavakisMathias Herrmann
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Apr 28, 2012·Arteriosclerosis, Thrombosis, and Vascular Biology·Anne BertlingBeate E Kehrel

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