1887

Abstract

The gene of encodes a protein Fbl that is 58 % identical to the clumping factor A (ClfA) of . The gene was present in eight clinical isolates of . When Fbl was expressed on the surface of it promoted adherence to immobilized fibrinogen and cell clumping in a fibrinogen solution. Purified recombinant Fbl region A bound to immobilized fibrinogen in a dose-dependent manner and inhibited the adherence of both Fbl-expressing and ClfA-expressing strains of to fibrinogen. Adherence of and Fbl to immobilized fibrinogen was also inhibited by rabbit anti-Fbl region A antibodies and rabbit anti-ClfA region A antibodies, as well as by human immunoglobulin with a high level of anti-ClfA antibodies. Alignment of the A domains of CflA and Fbl revealed that all of the ClfA residues implicated in binding to the -chain of fibrinogen are conserved in Fbl. Nevertheless Fbl had a tenfold lower affinity for fibrinogen, suggesting that sequence differences that occur elsewhere in the protein, possibly in -strand E of domain N2, affect ligand binding.

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2004-11-01
2019-10-13
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