title: Vitronectin-binding staphylococci enhance surface-associated complement activation.
abstract: Coagulase-negative staphylococci are well recognized in medical device-associated infections. Complement activation is known to occur at the biomaterial surface, resulting in unspecific inflammation around the biomaterial. The human serum protein vitronectin (Vn), a potent inhibitor of complement activation by formation of an inactive terminal complement complex, adsorbs to biomaterial surfaces in contact with blood. In this report, we discuss the possibility that surface-immobilized Vn inhibits complement activation and the effect of Vn-binding staphylococci on complement activation on surfaces precoated with Vn. The extent of complement activation was measured with a rabbit anti-human C3c antibody and a mouse anti-human C9 antibody, raised against the neoepitope of C9. Our data show that Vn immobilized on a biomaterial surface retains its ability to inhibit complement activation. The additive complement activation-inhibitory effect of Vn on a heparinized surface is very small. In the presence of Vn-binding strain, Staphylococcus hemolyticus SM131, complement activation on a surface precoated with Vn occurred as it did in the absence of Vn precoating. For S. epidermidis 3380, which does not express binding of Vn, complement activation on a Vn-precoated surface was significantly decreased. The results could be repeated on heparinized surfaces. These data suggest that Vn adsorbed to a biomaterial surface may serve to protect against surface-associated complement activation. Furthermore, Vn-binding staphylococcal cells may enhance surface-associated complement activation by blocking the inhibitory effect of preadsorbed Vn.
authors.affiliation: Department of Medical Microbiology, Lund University, Sweden.
authors.forename: F
authors.initials: F
authors.lastname: Lundberg
authors.forename: T
authors.initials: T
authors.lastname: Lea
authors.forename: A
authors.initials: A
authors.lastname: Ljungh
mesh_terms: D000818:Animals; D001422:Bacterial Adhesion; D001665:Binding Sites; D003167:Complement Activation; D006801:Humans; D051379:Mice; D011817:Rabbits; D013210:Staphylococcus / Q000502:physiology*; D019096:Vitronectin / Q000378:metabolism*
chemical_list: D019096:Vitronectin