title: Assemblies of pore-forming toxins visualized by atomic force microscopy.
abstract: A number of pore-forming toxins (PFTs) can assemble on lipid membranes through their specific interactions with lipids. The oligomeric assemblies of some PFTs have been successfully revealed either by electron microscopy (EM) and/or atomic force microscopy (AFM). Unlike EM, AFM imaging can be performed under physiological conditions, enabling the real-time visualization of PFT assembly and the transition from the prepore state, in which the toxin does not span the membrane, to the pore state. In addition to characterizing PFT oligomers, AFM has also been used to examine toxin-induced alterations in membrane organization. In this review, we summarize the contributions of AFM to the understanding of both PFT assembly and PFT-induced membrane reorganization. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale.
authors.affiliation: Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan.
authors.forename: Neval
authors.initials: N
authors.lastname: Yilmaz
authors.affiliation: Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan; INSERM U106-Université Lyon1, 69621 Villeurbanne, France. Electronic address: kobayasi@riken.jp.
authors.forename: Toshihide
authors.initials: T
authors.lastname: Kobayashi
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D006801:Humans; D018625:Microscopy, Atomic Force; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D052899:Pore Forming Cytotoxic Proteins
keywords: AFM imaging; High resolution; Oligomer; Phase boundary; Real time; Supported lipid bilayer