Lehrstuhl Zellbiologie, Universität Konstanz, Germany.
Eur J Cell Biol. 2011 Nov;90(11):891-6. doi: 10.1016/j.ejcb.2011.03.001. Epub 2011 May 10.
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.
通过整联蛋白家族的细胞黏附分子入侵哺乳动物细胞是细菌发病机制中的一个常见主题。虽然有些微生物直接与整合素结合，但其他病原体，如金黄色葡萄球菌，通过纤维连接蛋白结合蛋白（FnBPs）间接地与这些受体结合。在这篇综述中，我们总结了 FnBPs 的结构-功能关系以及这些蛋白在体内发病机制中的作用的最新观点。重点将放在胆固醇和鞘脂丰富的膜微区在纤维连接蛋白结合细菌整合素起始摄取中的作用以及 caveolin-1 在这一过程中的惊人抑制功能的最新发现上。对纤维连接蛋白结合的金黄色葡萄球菌感染宿主细胞的详细机制理解不仅可以作为其他纤维连接蛋白结合的致病性细菌的范例，还可能揭示配体占据的整合素内吞作用的生理调节。
