tailieunhanh - Báo cáo khoa học: Interaction of ostreolysin, a cytolytic protein from the edible mushroom Pleurotus ostreatus, with lipid membranes and modulation by lysophospholipids

Ostreolysin is a 16-kDa cytolytic protein specifically expressed in primordia and fruiting bodies of the edible mushroomPleurotus its interaction with lipid membranes,we compared its effects on mamma-lian cells,on vesicles preparedwith either pure lipids or total lipid extracts,and on dispersions of lysophospholipids or fatty acids. | Eur. J. Biochem. 270 1199-1210 2003 FEBS 2003 doi Interaction of ostreolysin a cytolytic protein from the edible mushroom Pleurotus ostreatus with lipid membranes and modulation by lysophospholipids Kristina Sepcic1 2 Sabina Berne2 Cristina Potrich1 Tom Turk2 Peter Macek2 and Gianfranco Menestrina1 lCNR-ITC Istituto di Biofisica - Sezione di Trento Povo Italy department of Biolog Biotechnical Faculty University of LjublCana Shm-ncu Ostreolysin is a 16-kDa cytolytic protein specifically expressed in primordia and fruiting bodies of the edible mushroom Pleurotus osU eatcs. To understand its interaction with lipid membranes we compared ite effecss cm mammalian cells on vesicles prepaired with either pure lipids or total lipid extracts and on dispersions of lysophospholipids or fatty acids. At nanomolar concentrations the protein lyeed human bovĩne and sheep eiy throcytes by a coUoíd-osmotíc mechanism compaiib e with the I ormaiion of cne s of 4 nm diameter and was cytotoxic to mammalian tumor cells. A search for lipid inhibitors of hemolysis revealed a strong effect of lysophospholipids and fatty acids occurring below their critical micellar concentration. This effect was distinct from the capacity of ostreolysin to bind to and permeabilize lipid membranes. In fact pormeabill a-ion of vesicles occurred only when they were prepared with lipids extracted from erythrocytes ami not with liidds xẦm l from P. oslrealus or pure lipid mixtures even if lysophosphoiipids or fatty acids were included. Interaction with lipid vesicles and their peameabilization correaited with an increase in the intrinsic fluorescence and a-helical content of the protein and with aggregation which were not deiecttd will lysophospholipids. It appears that either an unknown lipid acceptor or a specific lipid complex is required for binding aggregation and pore formation. The inhibitory effect of lysophospholipids may reflect a regulatory role for these components on

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