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金黄色葡萄球菌α-毒素诱导的离子通道结构

The structure of Staphylococcus aureus alpha-toxin-induced ionic channel.

作者信息

Krasilnikov O V, Sabirov R Z, Ternovsky V I, Merzliak P G, Tashmukhamedov B A

机构信息

Institute of Physiology, Academy of Sciences of the UzSSR, Tashkent.

出版信息

Gen Physiol Biophys. 1988 Oct;7(5):467-73.

PMID:2466732
Abstract

Polyethylene glycols (PEG) with molecular weight less than or equal to 3000 were shown to effectively protect human erythrocytes from osmotic lysis induced by alpha-staphylotoxin (ST). PEG with MW less than 3000 do not change the conductivity of ion channels induced by ST in bilayer lipid membranes (BLM). Changing the bilayer from a pure phosphatidylcholine (PC) to a negatively charged phosphatidylserine (PS) film results in an asymmetry of the current-voltage characteristics. This is evidenced by the asymmetrical position of the ST-channel pore in bilayer membranes. The results obtained allow to conclude that the ST-channel is an interprotein pore filled with water (with an inner diameter of 2.5-3 nm and a length of approximately 10 nm). It is composed of six molecules of alpha-toxin from Staphylococcus aureus. The ST-channel incorporates into a membrane with only one mouth in contact with the polar lipid heads and the other one protruding 4.5-5 nm from the bilayer plane in water solution.

摘要

分子量小于或等于3000的聚乙二醇(PEG)被证明能有效保护人类红细胞免受α-葡萄球菌肠毒素(ST)诱导的渗透裂解。分子量小于3000的PEG不会改变双层脂质膜(BLM)中由ST诱导的离子通道的电导率。将双层膜从纯磷脂酰胆碱(PC)改为带负电荷的磷脂酰丝氨酸(PS)膜会导致电流-电压特性不对称。这由双层膜中ST通道孔的不对称位置证明。所得结果表明,ST通道是一个充满水的蛋白间孔(内径为2.5 - 3纳米,长度约为10纳米)。它由六个金黄色葡萄球菌α-毒素分子组成。ST通道融入膜中时,只有一个口与极性脂质头部接触,另一个口在水溶液中从双层平面突出4.5 - 5纳米。

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The structure of Staphylococcus aureus alpha-toxin-induced ionic channel.金黄色葡萄球菌α-毒素诱导的离子通道结构
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