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                <term xml:lang="en">Pore-forming protein</term>
                <term xml:lang="en">Pleurotus ostreatus</term>
                <term xml:lang="en">Membrane attack complex/perforin (MACPF) domain</term>
                <term xml:lang="en">Electrophysiology</term>
              </keywords>
              <classCode scheme="mesh">Animals</classCode>
              <classCode scheme="mesh">CHO Cells</classCode>
              <classCode scheme="mesh">Fungal Proteins</classCode>
              <classCode scheme="mesh">Hemolysin Proteins</classCode>
              <classCode scheme="mesh">Hemolysis</classCode>
              <classCode scheme="mesh">Membrane Potentials</classCode>
              <classCode scheme="mesh">Mice</classCode>
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              <classCode scheme="mesh">Patch-Clamp Techniques</classCode>
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              <classCode scheme="mesh">Cattle</classCode>
              <classCode scheme="mesh">Cell Line, Tumor</classCode>
              <classCode scheme="mesh">Cell Membrane</classCode>
              <classCode scheme="mesh">Cell Membrane Permeability</classCode>
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              <classCode scheme="mesh">Cricetulus</classCode>
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              <p>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.</p>
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