The multifunctional human glycoprotein vitronectin (Vn) plays a significant role in cell
migration, tissue repair and regulation of membrane attack complex (MAC) formation. It also …

By interacting with components of the human host, including extracellular matrix (ECM)
proteins, Streptococcus pneumoniae has evolved various strategies for colonization. Here …

Vitronectin is a multifunctional glycoprotein present in blood and in the extracellular matrix. It
binds glycosaminoglycans, collagen, plasminogen and the urokinase-receptor, and also …

Tissue homeostasis depends on spatially and temporally controlled expression of
multifunctional adhesive glycoproteins and their cellular counter receptors, and on a tight …

Adherence of Streptococcus pneumoniae is directly mediated by interactions of adhesins
with eukaryotic cellular receptors or indirectly by exploiting matrix and serum proteins as …

Binding of microbial pathogens to host vitronectin (Vtn) is a common theme in the
pathogenesis of invasive infections. In this study, we characterized the role of Vtn in the …

Vitronectin (Vn) is a major adhesive glycoprotein in blood. However, many of the functions of
Vn are regulated by its conformational state and degree of multimerization. Here, the ability …

Vitronectin is a major adhesive glycoprotein found in the circulation as well as associated
with certain extracellular sites. Vitronectin was initially described as" serum spreading …

Summary Vitronectin (= complement S-protein) belongs to the group of structurally and
functionally homologous adhesive proteins (fibrinogen, fibronectin, von Willebrand factor) …

Several bacterial pathogens including Neisseria gonorrhoeae bind the human serum
glycoprotein vitronectin. We aimed at defining the gonococcal receptor for vitronectin …