Integrin-mediated internalization of Staphylococcus aureus does not require vinculin
1 Lehrstuhl Zellbiologie, Universität Konstanz, Postfach X908, 78457, Konstanz, Germany
2 Konstanz Research School Chemical Biology, Universität Konstanz, 78457, Konstanz, Germany
3 Hannover Medical School, Dept. of Paediatric Kidney, Liver and Metabolic Diseases, 30625, Hannover, Germany
Citation and License
BMC Cell Biology 2013, 14:2 doi:10.1186/1471-2121-14-2Published: 7 January 2013
Disease manifestations of Staphylococcus aureus are connected to the fibronectin (Fn)-binding capacity of these Gram-positive pathogens. Fn deposition on the surface of S. aureus allows engagement of α5β1 integrins and triggers uptake by host cells. For several integrin- and actin-associated cytoplasmic proteins, including FAK, Src, N-WASP, tensin and cortactin, a functional role during bacterial invasion has been demonstrated. As reorganization of the actin cytoskeleton is critical for bacterial entry, we investigated whether vinculin, an essential protein linking integrins with the actin cytoskeleton, may contribute to the integrin-mediated internalization of S. aureus.
Complementation of vinculin in vinculin -/- cells, vinculin overexpression, as well as shRNA-mediated vinculin knock-down in different eukaryotic cell types demonstrate, that vinculin does not have a functional role during the integrin-mediated uptake of S. aureus.
Our results suggest that vinculin is insignificant for the integrin-mediated uptake of S. aureus despite the critical role of vinculin as a linker between integrins and F-actin.