1887

Abstract

Fibronectin binding is considered to be an important virulence factor in streptococcal infections. Adhesion of the oral bacterium to immobilized forms of fibronectin is mediated, in part, by a high molecular mass wall-anchored protein designated CshA. In this study, a second fibronectin-binding protein of is described that has been designated as FbpA (627 kDa). This protein, which is encoded by a gene located immediately downstream of the gene, shows 85 and 81% identity to the fibronectin-binding proteins PavA, of , and FBP54, of , respectively. Purified recombinant FbpA bound to immobilized human fibronectin in a dose-dependant manner, and isogenic mutants in which the gene was inactivated were impaired in their binding to fibronectin. This effect was apparent only for cells in the exponential phase of growth, and was associated with reduced surface hydrophobicity and the surface expression of CshA. Cells in the stationary phase of growth were unaffected in their ability to bind to fibronectin. By utilizing gene promoter fusions with (encoding chloramphenicol -acetyltransferase), it was demonstrated that expression was down-regulated during the exponential phase of growth in the mutant. Expression of , but not , was sensitive to atmospheric O levels, and was found to be up-regulated in the presence of elevated O levels. The results suggest that FbpA plays a regulatory role in the modulation of CshA expression and, thus, affects the adhesion of to fibronectin.

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2002-06-01
2024-04-25
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