Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis.

Journal article

Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes.

Authors: Husmann, M; Beckmann, E; Boller, K; Kloft, N; Tenzer, S

• Publication status: Published
• Journal: FEBS letters
• Volume: 583
• Issue: 2
• Pages: 337-344
• Publication date: 2009-01-01
• DOI: 10.1016/j.febslet.2008.12.028
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Cell Line; Hemolysin Proteins; Animals; COS Cells; Exocytosis; Endocytosis; Bacterial Toxins; Cercopithecus aethiops; Mutation; Macrolides; Endosomes; Humans; Cell Nucleus