Adhesion of Streptococcus gallolyticus strains to extracellular matrix proteins.

Fourteen pigeon Streptococcus gallolyticus strains of differing virulence, were tested for their ability to adhere to immobilised fibronectin, collagen types I, III and IV. Eight, 2 and 13 strains were able to bind fibronectin, collagen types III and IV, respectively. None of the strains adhered to collagen type I. Heat treatment, proteolytic digestion or periodate treatment reduced the binding of S. gallolyticus to fibronectin and collagen type IV, suggesting that surface receptors contain proteins and carbohydrates. Although binding to these extracellular matrix proteins can play a role in the pathogenesis of streptococcosis in pigeons, binding properties could not be related to virulence, indicating that other factors determine differences in virulence among pigeon S. gallolyticus strains. Adhesion to collagen type IV may account in part for the distribution pattern of the lesions observed in naturally and experimentally infected pigeons.