Permeability characteristics of cell-membrane pores induced by ostreolysin A/pleurotolysin B,binary pore-forming proteins from the oyster mushroom |
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| Authors: | Sé bastien Schlumberger,Katarina Črnigoj Kristan,Katja Ota,Robert Frangež,Jordi Molgό,Kristina Sepčić,Evelyne Benoit,Peter Maček |
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| Affiliation: | 1. Laboratoire de Neurobiologie et Développement – UPR3294, Institut de Neurobiologie Alfred Fessard (INAF) – FRC2118, Centre National de la Recherche Scientifique (CNRS), 91198 Gif sur Yvette, France;2. Institute of Physiology, Medical Faculty, University of Maribor, 2000 Maribor, Slovenia;3. Department of Biology, Biotechnical Faculty, University of Ljubljana, 1000 Ljubljana, Slovenia;4. Institute of Physiology, Pharmacology and Toxicology, Veterinary Faculty, University of Ljubljana, 1000 Ljubljana, Slovenia |
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| Abstract: | Proteins from the oyster mushroom, 15 kDa ostreolysin A (OlyA), and 59 kDa pleurotolysin B (PlyB) with a membrane attack complex/perforin (MACPF) domain, damage cell membranes as a binary cytolytic pore-forming complex. Measurements of single-channel conductance and transmembrane macroscopic current reveal that OlyA/PlyB form non-selective ion-conducting pores with broad, skewed conductance distributions in N18 neuroblastoma and CHO-K1 cell membranes. Polyethylene-glycol 8000 (hydrodynamic radius of 3.78 nm) provides almost complete osmotic protection against haemolysis, which strongly suggests a colloid-osmotic type of erythrocyte lysis. Our data indicate that OlyA/PlyB form transmembrane pores of varied sizes, as other pore-forming proteins with a MACPF domain. |
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| Keywords: | Electrophysiology Membrane attack complex/perforin (MACPF) domain Pore-forming protein Pleurotus ostreatus |
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