Staphylococcus aureus autolysins interact with caprine vitronectin without involving the heparin binding domain and the second arginine-glycine-aspartic acid motif of the host protein.

Many bacteria exploit host proteins for their colonization. Vitronectin (Vn), present in the blood and extracellular matrix, is one such protein that acts as a bridge between the bacteria and the host tissues leading to infection. In this study, Vn binding protein of Staphylococcus aureus (COL strain) (SaVnBP) has been characterized as autolysin(s) based on mass spectrometry data and the ability of these proteins to degrade S.

Identification of second arginine-glycine-aspartic acid motif of ovine vitronectin as the complement C9 binding site and its implication in bacterial infection.

Vitronectin (Vn), a multifunctional protein of blood and extracellular matrix, interacts with complement C9. This interaction may modulate innate immunity. Details of Vn-C9 interactions are limited.