H. Ostolaza et al., RELEASE OF LIPID VESICLE CONTENTS BY THE BACTERIAL PROTEIN TOXIN ALPHA-HEMOLYSIN, Biochimica et biophysica acta, 1147(1), 1993, pp. 81-88
Alpha-Haemolysin is a protein toxin (107 kDa) secreted by some pathoge
nic strains of E. coli. It binds to mammalian cell membranes, disrupti
ng cellular activities and lysing cells. This paper describes the mech
anism of alpha-haemolysin-induced membrane leakage, from experiments i
n which extrusion large unilamellar vesicles, loaded with fluorescent
solutes, are treated with purified toxin. The results show that the to
xin does not require of any membrane receptor to exert its activity, t
hat vesicles become leaky following an 'all-or-none' mechanism, and th
at leakage occurs through a non-osmotic detergent-like bilayer disrupt
ion induced by the protein. Small pores formed by monomeric alpha-haem
olysin, as described by other authors, do not appear to be related to
the process of membrane disruption. Instead, the experimental data wou
ld be in agreement with the idea of oligomeric assemblies being requir
ed to produce release of solutes from a single vesicle.