γ-Hemolysins are bicomponent β-barrel pore forming toxins produced by Staphylococcus aureus as water-soluble monomers, which assemble into oligomeric pores on the surface of lipid bilayers. Here, after investigating the oligomeric structure of γ-hemolysins on supported lipid bilayers (SLBs) by atomic force microscopy (AFM), we studied the effect produced by this toxin on the structure of SLBs. We found that oligomeric structures with different number of monomers can assemble on the lipid bilayer being the octameric form the most stable one. Moreover, in this membrane model we found that γ-hemolysins can form clusters of oligomers inducing a curvature in the lipid bilayer, which could probably enhance the aggressiveness of these toxins at high concentrations.

γ-Hemolysin oligomeric structure and effect of its formation on supported lipid bilayers: An AFM Investigation / Alessandrini, Andrea; G., Viero; M., Dalla Serra; G., Prévost; P., Facci. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 1828:(2012), pp. 405-411. [10.1016/j.bbamem.2012.09.027]

γ-Hemolysin oligomeric structure and effect of its formation on supported lipid bilayers: An AFM Investigation.

ALESSANDRINI, Andrea;
2012

Abstract

γ-Hemolysins are bicomponent β-barrel pore forming toxins produced by Staphylococcus aureus as water-soluble monomers, which assemble into oligomeric pores on the surface of lipid bilayers. Here, after investigating the oligomeric structure of γ-hemolysins on supported lipid bilayers (SLBs) by atomic force microscopy (AFM), we studied the effect produced by this toxin on the structure of SLBs. We found that oligomeric structures with different number of monomers can assemble on the lipid bilayer being the octameric form the most stable one. Moreover, in this membrane model we found that γ-hemolysins can form clusters of oligomers inducing a curvature in the lipid bilayer, which could probably enhance the aggressiveness of these toxins at high concentrations.
2012
1828
405
411
γ-Hemolysin oligomeric structure and effect of its formation on supported lipid bilayers: An AFM Investigation / Alessandrini, Andrea; G., Viero; M., Dalla Serra; G., Prévost; P., Facci. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - STAMPA. - 1828:(2012), pp. 405-411. [10.1016/j.bbamem.2012.09.027]
Alessandrini, Andrea; G., Viero; M., Dalla Serra; G., Prévost; P., Facci
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/810894
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