Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870622 | FEBS Letters | 2014 | 6 Pages |
Abstract
Proteins from the oyster mushroom, 15Â kDa ostreolysin A (OlyA), and 59Â 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 3.78Â 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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Authors
Sébastien Schlumberger, Katarina Ärnigoj Kristan, Katja Ota, Robert Frangež, Jordi MolgÏ, Kristina SepÄiÄ, Evelyne Benoit, Peter MaÄek,