Adherence of Staphylococcus aureus is enhanced by an endogenous secreted protein with broad binding activity.

A novel mechanism for enhancement of adherence of Staphylococcus aureus to host components is described. A secreted protein, Eap (extracellular adherence protein), was purified from the supernatant of S. aureus Newman and found to be able to bind to at least seven plasma proteins, e.g., fibronectin, the alpha-chain of fibrinogen, and prothrombin, and to the surface of S. aureus. Eap bound much less to cells of Staphylococcus epidermidis, Streptococcus mutans, or Escherichia coli. The protein can form oligomeric forms and is able to cause agglutination of S. aureus. Binding of S. aureus to fibroblasts and epithelial cells was significantly enhanced by addition of Eap, presumably due to its affinity both for plasma proteins on the cells and for the bacteria.