Probing phosphoethanolamine-containing lipids in membranes with duramycin/cinnamycin and aegerolysin proteins.
In this mini-review, we summarize current knowledge about the lipid-binding characteristics of two types of toxins used to visualize the membrane distribution of phosphoethanolamine-containing lipid species: the glycerophospholipid, phosphatidylethanolamine (PE) and the sphingolipid, ceramide phosphoethanolamine (CPE). The lantibiotic cinnamycin and the structurally-related peptide duramycin produced by some Gram-positive bacteria were among the first toxins characterized by their specificity for PE which is widely present in animal kingdoms from bacteria to mammals. These toxins promoted their binding to PE-containing membranes by changing membrane curvature and by inducing transbilayer lipid movement. The recognition of the conical shape and negative curvature adopted by the PE species within the membrane, is important to understand how lipid-peptide interaction can occur. Three mushroom-derived proteins belonging to the aegerolysin family, pleurotolysin A2, ostreolysin and erylysin A were recently described as efficient tools to visualize the membrane distribution of CPE which is found in trace amounts in mammalian cells but in higher amounts in some developmental stages of lower eukaryotes like Trypanosoma and in invertebrates such as Drosophila. The recent development of lantibiotic-based PE-specific and aegerolysin-based CPE-specific probes is useful to visualize and specify the role of these lipids in various pathophysiological events such as cell division, apoptosis, tumor vasculature and parasite developmental stages.
UMR INSERM 1060-INSA Lyon-University Claude Bernard, Laboratoire CarMeN, Batiment IMBL, 15 avenue Jean Capelle, 69621, Villeurbanne cedex, France; Lipid Biology Laboratory, RIKEN, Wako, Saitama, 351-0198, Japan. Electronic address: francoise.hullin-matsuda@inserm.fr.
Françoise
F
Hullin-Matsuda
Lipid Biology Laboratory, RIKEN, Wako, Saitama, 351-0198, Japan. Electronic address: makino@riken.jp.
Asami
A
Makino
Lipid Biology Laboratory, RIKEN, Wako, Saitama, 351-0198, Japan. Electronic address: mmurate@riken.jp.
Motohide
M
Murate
Lipid Biology Laboratory, RIKEN, Wako, Saitama, 351-0198, Japan; UMR 7213 CNRS, University of Strasbourg, 67401, Illkirch, France. Electronic address: toshihide.kobayashi@unistra.fr.
Toshihide
T
Kobayashi
D000818:Animals; D001430:Bacteriocins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D001667:Binding, Competitive / Q000187:drug effects; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D004983:Ethanolamines / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D006460:Hemolysin Proteins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D010714:Phosphatidylethanolamines / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects
D001430:Bacteriocins; D004983:Ethanolamines; D005656:Fungal Proteins; D006460:Hemolysin Proteins; D010455:Peptides; D010456:Peptides, Cyclic; D010714:Phosphatidylethanolamines; C461279:aegerolysin; C040522:duramycin; C000485:cinnamycin; C483858:phosphatidylethanolamine; C005448:phosphorylethanolamine
Ceramide phosphoethanolamine; Erylysin; Lantibiotics; Ostreolysin; Phosphatidylethanolamine; Pleurotolysin A2