Mode of binding of fibrinogen, fibronectin and iron-binding proteins by animal enterococci.

Sixty-two animal enterococci were examined for their binding of bovine fibrinogen, porcine fibronectin, bovine lactoferrin, bovine apotransferrin and human holotransferrin in the particle agglutination assay (PAA). Individual strains expressed binding of selected glycoproteins to various degrees (0, 1, 2, 3), whereas bovine fibrinogen binding of enterococci from goats, rabbits and rodents was the strongest (3) in general. Porcine fibronectin was bound weakly (1 or 2) by enterococci from horses, dogs, poultry, rabbits and rodents, while most of the goat isolates and half of the dog feed isolates did not bind fibronectin (0). Bovine lactoferrin was bound especially by the isolates from rodents and rabbits. Bovine apotransferrin was bound very weakly (1) by only a few isolates. Human holotransferrin was bound to a greater extent than apotransferrin by some isolates from rabbits and rodents. Since multiresistant strains are preferred in our binding studies, enterococci were also examined for their antibiotic resistance pattern. Almost all investigated isolates were resistant at least to one antibiotic. However, some strains displayed resistance to five or six antibiotics of 10 antibiotics tested. In a study of the inhibitory effect of heparin, porcine mucin and hyaluronic acid, the greatest effect was observed after heparin treatment of bacterial cells. These observations, as well as the expression of heparin binding by most strains, may suggest that at least one mode of enterococcal attachment utilizes glycosaminoglycan chains present on the surface of adherent cells.