Molecular mechanisms of action of sphingomyelin-specific pore-forming toxin, lysenin.

Neval Yilmaz, Akiko Yamaji-Hasegawa, Françoise Hullin-Matsuda, Toshihide Kobayashi

Journal: Seminars in cell & developmental biology 2018;73():188-198

PMID: 28751253

Abstract

Lysenin, which is an earthworm toxin, strongly binds to sphingomyelin (SM). Lysenin oligomerizes on SM-rich domains and can induce cell death by forming pores in the membrane. In this review, the assembly of lysenin on SM-containing membranes is discussed mostly on the basis of the information gained by atomic force microscopy (AFM). AFM data show that lysenin assembles into a hexagonal close packed (hcp) structure by rapid reorganization of its oligomers on an SM/cholesterol membrane. In case of a phase-separated membrane of SM, lysenin induces phase mixing as a result of pore formation in SM-rich domains, and consequently its hcp assembly covers the entire membrane. Besides the lytic action, lysenin is important as an SM marker and its pore has the potential to be used as a biosensor in the future. These points are also highlighted in this review.

Copyright © 2017 Elsevier Ltd. All rights reserved.

Address: Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan; Enzyme Research Team, CSRS, RIKEN, Wako, Saitama 351-0198, Japan. Electronic address: [email protected].; Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan; Laboratory for Molecular Membrane Neuroscience, BSI, RIKEN, Wako, Saitama 351-0198, Japan.; Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan; Univ-Lyon, CarMeN laboratory, Inserm U1060, INRA U1397, Université Claude Bernard Lyon 1, INSA Lyon, 69621, Villeurbanne, France.; Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan; UMR7213 CNRS, Laboratoire de Biophotonique et Pharmacologie, Faculté de Pharmacie, Université de Strasbourg, 74 route du Rhin, 67401 Illkirch, France. Electronic address: [email protected].

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