In contrast, binding was not inhibited by a bacterial lysate from an osteopontin A gtll lysogen, nor by N-linked oligosaccharide isolated from bone sialoprotein or by proteoglycan from rat chondrosarcoma containing clustered 0-linked oligosaccharides of the same structure as those of bone sialoprotein. These results indicate that the major staphylococcal-binding site resides in the bone sialoprotein core protein and not in the carbohydrate side chains. No inhibition of bone sialoprotein binding could be detected for whole human serum or purified plasma proteins such as fibronectin, fibrinogen and IgG. Likewise, staphylococcal protein A or rat collagen type I did not inhibit the binding of bone sialoprotein. The latter results indicate that the binding site for bone sialoprotein on staphylococcal cells was not any of the hitherto described staphylococcal cell-surface proteins. Binding data indicated an average of 1000 bone-sialoprotein-binding sites/bacterial cell.
Staphylococcus aureus cells have been shown to possess surface-associated proteins with affinity for soluble fibronectin. We have investigated the ability of these surface proteins to mediate attachment to immobilized fibronectin and collagen. Attachment was quantified by determination of bacterial ATP in a bioluminescence assay. The ability to attach to fibronectinor collagen-coated plastic surfaces was investigated for four S. aureus strains: Cowan 1, Newman, SA113(83A), and Wood 46. Cells from the different strains varied in their attachment properties, but all cells except those of strain Wood 46 attached readily to substrates coated with fibronectin. Only cells from strain Cowan 1 attached reproducibly to collagen-coated substrates in the absence of fibronectin. The attachment of cells from strain SA113(83A) to fibronectin-coated surfaces was shown to be dependent on time, fibronectin concentration, and bacterial growth phase. Soluble fibronectin or NH2-terminal fibronectin fragment (Mr, 29,000) disturbed the attachment to surfaces coated with fibronectin bound to denatured collagen type I. The attachment process to such substrates was also effectively inhibited by preincubating the substrate with fibronectin-binding proteins isolated from S. aureus Newman and SA113 (83A) and purified with affinity chromatography.
Two high molecular weight staphylococcal proteins, fibronectin‐binding protein and a M 200 000 protein, were investigated as antigens for serodiagnosis of staphylococcal infections. Sera from patients with staphylococcal infections and from controls were subjected to immunoblot analysis with staphylococcal lysate proteins to identify staphylococcal antigens to which patients with staphylococcal infections specifically exhibited antibodies. On such protein was found in the M 200 000 region. This protein was purified and used as antigen in ElISA and compared with other antigens, namely fibronectin‐binding protein(s) (FNBP, M, 185 000), α‐toxin and teichoic acid. Sera from patients with staphylococcal infections contained antibodies to the high molecular weight proteins in higher titers than sera from patients with non‐staphylococcal infections or healthy subjects. Based on their amino‐acid compositions and different abilities to bind fibronectin it was concluded that the M 200 000 protein and FNBP were not identical.
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