Integrin-mediated uptake of fibronectin-binding bacteria

Abstract

Invasion of mammalian cells via cell adhesion molecules of the integrin family is a common theme in bacterial pathogenesis. Whereas some microorganisms directly bind to integrins, other pathogens such as Staphylococcus aureus indirectly engage these receptors via fibronectin-binding proteins (FnBPs). In this review, we summarize the structure-function relationship of FnBPs and the current view of the role of these proteins during pathogenesis in vivo. A major focus will be on recent findings on the role of cholesterol- and sphingolipid-rich membrane microdomains for integrin-initiated uptake of fibronectin-binding bacteria and the surprising inhibitory function of caveolin-1 in this process. The detailed mechanistic understanding of host cell invasion by fibronectin-binding S. aureus can not only serve as a paradigm for other fibronectin-binding pathogenic bacteria, but might also reveal the physiological regulation of endocytosis of ligand-occupied integrins.