title: 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.
authors.affiliation: Lehrstuhl Zellbiologie, Universität Konstanz, Germany.
authors.forename: Christine
authors.initials: C
authors.lastname: Hoffmann
authors.forename: Knut
authors.initials: K
authors.lastname: Ohlsen
authors.forename: Christof R
authors.initials: CR
authors.lastname: Hauck
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001419:Bacteria / Q000378:metabolism* / Q000472:pathogenicity*; D001422:Bacterial Adhesion; D004705:Endocytosis; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D021962:Membrane Microdomains; D051379:Mice; D013211:Staphylococcus aureus / Q000166:cytology / Q000378:metabolism* / Q000472:pathogenicity*; D013329:Structure-Activity Relationship
chemical_list: D018829:Adhesins, Bacterial; D016023:Integrins; C078635:fibronectin-binding proteins, bacterial