Abstract
The assembling of the sphingomyelin (SM)-binding pore-forming toxin (PFT), lysenin, to SM/cholesterol bilayer was examined by high-speed atomic force microscopy (HS-AFM) [1]. The HS-AFM images of SM/cholesterol bilayer preincubated with lysenin exhibited the hexagonal close packed (hcp) assembly of lysenin oligomers (Fig. 1A). The in-situ AFM images revealed that the formation of the hcp structure took place quickly (Fig. 1B). Before the full coverage of the membrane surface with a stable hcp assembly of lysenin oligomers, most of the oligomers underwent reorganization either by dissociating into monomers or by rapidly diffusing along the membrane in less than a second. The assembling of lysenin oligomers was also followed on SM/DOPC/cholesterol bilayer. Oligomers firstly formed at the edges of the SM-rich domains and covered these domains similarly to the SM/cholesterol bilayer. Our results revealed the dynamic nature of the oligomers of a lipid binding toxin during its assembling on SM-containing membranes.Reference[1] N. Yilmaz, T. Yamada, P. Greimel, T. Uchihashi, T. Ando, and T. Kobayashi, Biophys. J. 105, 1397-1405 (2013).View Large Image | View Hi-Res Image | Download PowerPoint Slide
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