Physical characterization of the pore forming cytolysine from Gardnerella vaginalis.

The cytolytic toxin (CTox) produced by Gardnerella vaginalis is able to form voltage-dependent cationic channels when incorporated in lipid membranes (Moran et al. (1991) FEBS Lett. 283, 317-320). Osmotic protection experiments show that toxin incorporated in human erythrocytes forms pores between 18 A and 28 A in diameter. A hypothesis of pore formation as a primary event to produce cytolysis is proposed. The CTox activity increases when cells are depolarized by increasing the extracellular K+ concentration, probably reflecting the voltage dependent character of CTox formed channels. The cytolytic effect of the toxin was prevented by low temperatures and was a function of the extracellular Ca2+ concentration, suggesting a Ca2+ influx as part of the lytic mechanism. Binding of CTox to erythrocytes was dependent on external Ca2+ and was less temperature-dependent. Dose-response analysis suggests cooperativity of the toxin for the lytic activity, although no direct evidence of oligomerization has been found.