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MBC in Press, published online ahead of print October 4, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0463

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Submitted on May 31, 2006
Revised on September 14, 2006
Accepted on September 26, 2006

Staphylococcus aureus Fibronectin Binding Protein-A Induces Motile Attachment Sites and Complex Actin Remodeling in Living Endothelial Cells

Andreas Schröder,*{dagger} Barbara Schröder,{ddagger}{sect} Bernhard Roppenser,* Stefan Linder,{ddagger} Bhanu Sinha,|| Reinhard Fässler,¶ and Martin Aepfelbacher*

*Institut für Medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Hamburg-Eppendorf, 20246 Hamburg, Germany; {dagger}Max von Pettenkofer-Institut and {ddagger}Institut für Prophylaxe der Kreislaufkrankheiten, Ludwig-Maximilians-Universität München, 80336 München, Germany; ||Institut für Medizinische Mikrobiologie, Universitätsklinikum Münster, 48149 Münster, Germany; Max-Planck-Institut für Biochemie, Abteilung für Molekulare Medizin, 82152 Martinsried, Germany

Monitoring Editor: Ralph Isberg

Staphylococcus aureus fibronectin binding protein-A (FnBPA) stimulates {alpha}5{beta}1-integrin signaling and actin rearrangements in host cells. This eventually leads to invasion of the staphylococci and their targeting to lysosomes. Employing live cell imaging we found that FnBPA-expressing staphylococci induce formation of fibrillar adhesion-like attachment sites and translocate together with them on the surface of human endothelial cells (velocity ~50 µm per hour). The translocating bacteria recruited cellular actin and Rab5 in a cyclic and alternating manner, suggesting unsuccessful attempts of phagocytosis by the endothelial cells. Translocation, actin recruitment and eventual invasion of the staphylococci was regulated by the fibrillar adhesion protein tensin. The staphylococci also regularly produced N-WASP-controlled actin comet tails that further propelled them on the cell surface (velocity up to 1000 µm per hour). Thus, S. aureus FnBPA produces attachment sites that promote bacterial movements but subvert actin- and Rab5 reorganisation during invasion. This may constitute a novel strategy of S. aureus to postpone invasion until its toxins become effective.

{sect}Present address: Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905.

Address correspondence to: Martin Aepfelbacher (m.aepfelbacher{at}uke.uni-hamburg.de)




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