Abstract
The assembly of the sphingomyelin (SM)-binding pore-forming toxin (PFT), lysenin, on SM/cholesterol bilayer was examined by high-speed atomic force microscopy (HS-AFM). Previous studies suggest that lysenin oligomerizes after binding to SM and forms a honeycomb structure. The HS-AFM images of SM/ cholesterol bilayer preincubated with lysenin exhibited the honeycomb assembly of the lysenin oligomers. The time-lapse AFM images revealed that the honeycomb formation took place quickly. During honeycomb formation most of the oligomers underwent reorganization either by dissociating into monomers or by rapidly diffusing along the membrane in less than a second. In the period of reorganization, the mobile oligomers arranged into a static, well-ordered lattice. Once this static layer was formed, the lysenin molecules were firmly bound to the SM/cholesterol bilayer and the oligomers neither dissociated nor diffused. Our results revealed the dynamic nature of the oligomers of a lipid binding toxin during honeycomb formation.
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