M. Flock et Ji. Flock, Rebinding of extracellular adherence protein Eap to Staphylococcus aureus can occur through a surface-bound neutral phosphatase, J BACT, 183(13), 2001, pp. 3999-4003
Extracellular adherence protein Eap secreted from Staphylococcus aureus was
previously found to enhance the adherence of S, aureus to eukaryotic cells
. This enhancement effect is due to the ability of Eap to rebind to S, aure
us and to bind to eukaryotic cells and several plasma and matrix proteins.
In this study we defined one potential binding target for Eap on the surfac
e of S, aureus, a surface-located neutral phosphatase. This phosphatase lac
ks an LPXTG region, but around 80% is retained on the cell surface. The sol
uble phosphatase can form a complex with Eap at a nonrandom molar ratio, an
d phosphatase activity is retained. The phosphatase can also bind to fibron
ectin. The cell surface-located portion presumably contributes to adherence
of S. aureus to fibronectin.