6533b834fe1ef96bd129ce55

RESEARCH PRODUCT

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

Wiesia BobkiewiczKlaus BollerMatthias HusmannSucharit BhakdiNicole KloftErik BeckmannHagan BayleyStefan TenzerClaudia Neukirch

subject

Staphylococcus aureusEndosomeBacterial ToxinsBiophysicsEndosomesBiologyEndocytosisHemolysin ProteinsBiochemistryα-ToxinExocytosisVirulence factorExocytosisCell LineHemolysin ProteinsStructural BiologyNucleated cellChlorocebus aethiopsGeneticsExtracellularAnimalsHumansMolecular BiologyCell NucleusBacterial pore forming toxinPore-forming toxinInnate defence mechanismCell BiologyEndocytosisCell biologyExosomeBiochemistryCOS CellsMutationMacrolides

description

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.

yearjournalcountryeditionlanguage
2008-11-14FEBS Letters
10.1016/j.febslet.2008.12.028http://dx.doi.org/10.1016/j.febslet.2008.12.028