|
|||||
|
|
Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis |
|
| Authors: | Matthias Husmann Erik Beckmann Nicole Kloft Wiesia Bobkiewicz Hagan Bayley |
| Affiliation: | a Institute of Medical Microbiology and Hygiene, Johannes Gutenberg-University Mainz, Hochhaus am Augustusplatz, 55131 Mainz, Germany b Paul Ehrlich-Institute, Department of Immunology, Morphology Section, 63225 Langen, Germany c Institute of Immunology, Johannes Gutenberg-University Mainz, 55131 Mainz, Germany d Chemical Research Laboratory, Chemical Biology Sub-Department, University of Oxford, Oxford OX1 3TA, England, UK |
| Abstract: | 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. |
| Keywords: | 1mer, α-toxin monomer 7mer, α-toxin heptamer CSPL, cell surface protein labeling IP, immunoprecipitation MVB, multivesicular bodies PFT, pore forming toxins SLO, streptolysin O Tbl, Trypan blue |
| 本文献已被 ScienceDirect 等数据库收录！ | |