The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins.

@article{Pdelacq1999TheSO,
  title={The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins.},
  author={J D P{\'e}delacq and Laurent Maveyraud and Gilles Pr{\'e}vost and Lamine Baba-Moussa and Arcelia Gonz{\'a}lez and Emmanuel Courcelle and William Shepard and Henri Monteil and Jean Samama and Lionel Mourey},
  journal={Structure},
  year={1999},
  volume={7 3},
  pages={277-87}
}
BACKGROUND Leucocidins and gamma-hemolysins are bi-component toxins secreted by Staphylococcus aureus. These toxins activate responses of specific cells and form lethal transmembrane pores. Their leucotoxic and hemolytic activities involve the sequential binding and the synergistic association of a class S and a class F component, which form hetero-oligomeric complexes. The components of each protein class are produced as non-associated, water-soluble proteins that undergo conformational… CONTINUE READING