Structural basis for pore-forming mechanism of staphylococcal α-hemolysin.

Staphylococcal α-hemolysin (α-HL) is a β-barrel pore-forming toxin (PFT) expressed by Staphylococcus aureus. α-HL is secreted as a water-soluble monomeric protein, which binds to target membranes and forms membrane-inserted heptameric pores. To explore the pore-forming mechanism of α-HL in detail, we determined the crystal structure of the α-HL monomer and prepore using H35A mutant and W179A/R200A mutant, respectively.

Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins.

Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the β-barrel formation process.

Preliminary X-ray crystallographic study of staphylococcal α-haemolysin monomer.

Staphylococcal α-haemolysin is a β-barrel pore-forming toxin expressed by Staphylococcus aureus. α-Haemolysin is secreted as a water-soluble monomeric protein which binds to target membranes and forms membrane-inserted heptameric pores. Although the crystal structures of the heptameric pore and monomer bound to an antibody have been determined, that of monomeric α-haemolysin without binder has yet to be elucidated.