Abstract
Staphylococcal leucotoxins result from the association of class S components and class F component inducing the activation and the permeabilization of the target cells. Like alpha-toxin, the leucotoxins are pore-forming toxins with more than 70% beta-sheet. This was confirmed by attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy. In addition, threonine 28 of a predicted and conserved beta-sheet at the N-terminal extremity of class S proteins composing leucotoxins aligns with histidine 35 of alpha-toxin, which has a key role in oligomerization of the final pore. Flow cytometry was used to study different aminoacid substitutions of the threonine 28 in order to evaluate its role in the biological activity of these class S proteins. Finally, results show that threonine 28 of the leucotoxin probably plays a role similar to that of histidine 35 of alpha-toxin. Mutations on this threonin largely influenced the secondary interaction of the class F component and led to inactive toxin.