Binding of bovine fibronectin to mastitis-causing Streptococcus agalactiae induces adherence to solid substrate but not phagocytosis by polymorphonuclear cells.

Streptococcus agalactiae is frequently associated with mastitis in cattle, and fibronectin is a host protein which interferes with infection, particularly at mucosal sites. The binding of bovine fibronectin to S. agalactiae was investigated by enzyme-linked immunosorbent assay (ELISA). Binding was time-dependent and dose-dependent. Most of the strains tested showed low ELISA activity, but some strains (six out of 17) had much higher activity. The highest-binding strains of S. agalactiae were able to adhere to bovine fibronectin-coated polystyrene. Adherence was inhibited by arginine or gelatin, but was slightly favored by soluble fibronectin. Fibronectin did not contribute to the opsonization (deposition of complement C3) and phagocytosis of the strain which bound the highest amount of fibronectin, even when polymorphonuclear cells were activated with serum-derived chemotaxin (C5a). These data suggest that fibronectin might promote tissue adherence but not phagocytosis of S. agalactiae in the mastitis process.