Mechanism of membrane permeabilization by sticholysin I, a cytolysin isolated from the venom of the sea anemone Stichodactyla helianthus

Biochemistry
M TejucaG Menestrina

Abstract

Actinaria cytolysins are very potent basic toxins isolated from the venom of sea anemones, which are supposed to exert their toxic activity through formation of oligomeric pores in the host plasma membrane. To gain insight into their mechanism of action, the interaction of Stichodactyla helianthus sticholysin I (St-I) with lipid bilayers was studied. St-I increased the permeability of calcein-loaded lipid vesicles composed of different phospholipids. The rate of permeabilization improved when sphingomyelin (SM) was introduced into phosphatidylcholine (PC) vesicles, reaching an optimum value at equimolar concentrations of these two phospholipids. It was also a function of the pH, showing a local maximum of activity between pH 8 and 9 and a marked decrease at pH 10 and 11. Under optimal conditions (e.g., PC:SM 1:1, pH 8, toxin to vesicle ratio < 200), most of the toxin is bound to the lipid phase. The reduced toxin effect at low and high SM content, or at high pH, is principally due to a decreased toxin binding. From the dose dependence of the permeabilization, at constant lipid concentration, it was inferred that St-I increases membrane permeability by forming oligomeric pores comprising at least three cytolysin monomers. The in...Continue Reading

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