Immunological Recognition of Fibronectin‐Binding Proteins of Staphylococcus aureus and Staphylococcus capitis, Strain LK499

Abstract

Antibodies to fibronectin-binding proteins (FnBPs) of Staphylococcus aureus, including binding domain of FnBPA, the D region, or the A-C regions of FnBPB were produced in rabbits and mice. These antibodies were used to characterize cell-associated FnBPs of S. aureus strain Cowan I, S. aureus strain U320 and a coagulase-negative Staphylococcus capitis strain LK 499 as well as extracellular FnBPs in culture supernatants of the strain U320. FnBPs of S. aureus were predominantly FnBPA, while FnBPB was hardly detected on the cells or in culture supernatant of these S. aureus strains. Moreover, S. capitis strain LK 499 possessed different FnBP(s) compared to S. aureus because the antibodies to S. aureus FnBPs did not recognize FnBP(s) on S. capitis.

Staphylococcus aureus fibronectin‐binding proteins (FnBPs)

“…Human plasma fibronectin was purified according to Vwnto & Vahieri (21). Binding of '*Wibronectin to staphylococci or to immobilized FnBPs, and blocking of binding in the presence of antibodies were performed as previously described (2, 8, 13,14).…”

Fibronectin binding by Propionibacterium acnes

“…In contrast to E. coli , Streptococci and other bacterial species [19], P. acnes recognizes the 150 kD fragment of Fn and not the N‐terminal of the 29 kD fragment. S. aureus strains have been shown to bind to a domain within the 150 kD fragment apart from the 29 kD fragment [20, 21]. The data that heparin could inhibit binding of the 150 kD fragment by >50% indicates that the binding domain is located close to the heparin binding domain within the 150 kD fragment of Fn.…”