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Elimination of a bacterial pore‐forming toxin by sequential endocytosis and exocytosis
Author(s) -
Husmann Matthias,
Beckmann Erik,
Boller Klaus,
Kloft Nicole,
Tenzer Stefan,
Bobkiewicz Wiesia,
Neukirch Claudia,
Bayley Hagan,
Bhakdi Sucharit
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.12.028
Subject(s) - endocytosis , exocytosis , virulence factor , extracellular , toxin , microbiology and biotechnology , pore forming toxin , anthrax toxin , staphylococcus aureus , context (archaeology) , chemistry , biofilm , endocytic cycle , biophysics , virulence , bacteria , biology , recombinant dna , microbial toxins , biochemistry , membrane , receptor , fusion protein , genetics , paleontology , gene
Staphylococcus aureus α‐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 β‐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 α‐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 .