The Staphylococcus aureus receptor for fibronectin.
The Staphylococcus aureus binding site for human fibronectin was determined by unique biologic assays based upon the specific adherence of the bacterium to nasal epithelial cells. Fibronectin treatment of S. aureus caused a reduction in adherence tallies on high granular and fully keratinized cells compared to controls (p less than 0.05; p less than 0.001). Spinous and low granular cells showed no significant differences. The cell wall materials N-acetyl-D-glucosamine, N-acetyl muramic acid, and protein A were unable to inhibit the coupling of fibronectin to S. aureus. Only ribitol teichoic acid had this property. Furthermore, fibronectin could neutralize the adherence-blocking ability of teichoic acid, which affects keratinized cells. Thus, teichoic acid seems to be a receptor for fibronectin.
D001665:Binding Sites; D002448:Cell Adhesion; D006801:Humans; D009297:Nasal Mucosa / Q000166:cytology; D011956:Receptors, Cell Surface / Q000032:analysis*; D017469:Receptors, Fibronectin; D013211:Staphylococcus aureus / Q000166:cytology*
D011956:Receptors, Cell Surface; D017469:Receptors, Fibronectin