Escherichia coli haemolysin forms voltage-dependent ion channels in lipid membranes.
The action of the 107 kDa hemolysin from Escherichia coli on planar lipid membranes was investigated. We report that a single toxin molecule can form a cation-selective, ion-permeable channel of large conductance in a planar phospholipid bilayer membrane. The conductance of the pore is proportional to that of the bulk solution, indicating that the channel is filled with water. A pore diameter of about 2 nm can be evaluated. The pore formation mechanism is voltage-dependent and essentially resembles that of pore-forming colicins; this implies that opening of the channel is dependent on transfer of an electrical charge through the membrane. We propose that the physiological effects of E. coli hemolysin result from its ability to form ion channels in the membrane of attacked cells, and show that there is quantitative agreement between the effects of this toxin on model membranes and its hemolytic properties.
D002118:Calcium / Q000378:metabolism; D004926:Escherichia coli / Q000032:analysis*; D006460:Hemolysin Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D007473:Ion Channels / Q000187:drug effects*; D008051:Lipid Bilayers / Q000378:metabolism*; D008564:Membrane Potentials; D010447:Peptide Hydrolases / Q000494:pharmacology; D010743:Phospholipids; D011188:Potassium / Q000378:metabolism; D012964:Sodium / Q000378:metabolism
D006460:Hemolysin Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D010743:Phospholipids; D012964:Sodium; D010447:Peptide Hydrolases; D011188:Potassium; D002118:Calcium