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For endocytosis and exocytosis, membranes transition between planar, budding,and vesicular topographies through nanoscale reorganization of lipids,proteins, and carbohydrates. However, prior attempts to understand the initialstages of nanoscale bending have been limited by experimental resolution.Through the implementation of polarized localization microscopy (PLM), thismanuscript reports the inherent membrane bending capability of cholera toxinsubunit B (CTxB) in quasi-one component supported lipid bilayers. Membrane budswere first detected with <50 nm radius, grew to >200 nm radius, and extendedinto longer tubules with dependence on the membrane tension and CTxBconcentration. Compared to the concentration of the planar supported lipidbilayers, CTxB was >10x more concentrated on the positive curvature top and>25x more concentrated on the negative Gaussian curvature neck of the nanoscalemembrane buds. This finding elucidates prior observations by correlating CTxBclustering and diffusion to CTxB-induced membrane bending. CTxB is frequentlyused as a marker for liquid-ordered lipid phases; however, the coupling betweenCTxB and membrane bending provides an alternate understanding of CTxB-inducedmembrane reorganization. Single-particle tracking was performed on both lipidsand CTxB to reveal the correlation between single-molecule diffusion, CTxBaccumulation, and membrane topography. Slowed lipid and CTxB diffusion wasobserved at the nanoscale buds locations, suggesting a local increase inmembrane viscosity or molecular crowding upon membrane bending. These resultssuggest inherent CTxB-induced membrane bending as a mechanism for initiatingCTxB internalization in cells that is initially independent of clathrin,caveolin, actin, and lipid phase separation.

Nanoscale membrane budding induced by CTxB on quasi-one component lipid bilayers detected by polarized localization microscopy