Isolated extracellular matrix-binding proteins, designated ClfB, SdrC,
SdrD and SdrE, and their corresponding amino acid and nucleic acid
sequences and motifs are described. The proteins, peptides, fragments
thereof or antigenic portions thereof are useful for the prevention,
inhibition, treatment and diagnosis of S. aureus infection and as
scientific research tools. Further, antibodies or antibody fragments to
the proteins, peptides, fragments thereof or antigenic portions thereof
are also useful for the prevention, inhibition, treatment and diagnosis
of S. aureus infection. In particular, the proteins or antibodies thereof
may be administered to wounds or used to coat biomaterials to act as
blocking agents to prevent or inhibit the binding of S. aureus to wounds
or biomaterials.ClfB is a cell-wall associated protein having a predicted
molecular weight of approximately 88 kDa and an apparent molecular weight
of approximately 124 kDa, which binds both soluble and immobilized
fibrinogen. ClfB binds both the alpha and beta chains of fibrinogen and
acts as a clumping factor. SdrC, SdrD and SdrE are cell-wall associated
proteins that exhibit cation-dependent ligand binding to the
extracellular matrix. It has been discovered that in the A region of
SdrC, SdrD, SdrE, ClfA and ClfB, there is a highly conserved amino acid
sequence that can be used to derive a consensus motif of TYTFTDYVD.