The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein
The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol-anchored protein
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DOI：
10.1046/j.1365-2958.1997.4691828.x
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发表时间：
1997-07-01
影响因子：
3.6
通讯作者：
Buckley, JT
中科院分区：
文献类型：
--
作者：
Cowell, S;Aschauer, W;Buckley, JT
大鼠红细胞的质膜含有47 kDa的糖蛋白，其以高亲和力结合通道形成毒素气溶素，并解释了这些细胞对毒素的敏感性。该受体的N端序列与数据库中的任何序列都不匹配，表明该受体是一种新的红细胞表面蛋白。然而，它与一组被认为参与ADP-核糖基转移反应的膜蛋白的N端具有相当大的同源性，这些蛋白质的一个共同特性是它们通过C-末端糖基磷脂酰肌醇（GPI）锚附着于质膜。通过用磷脂酰肌醇特异性磷脂酶C处理大鼠红细胞，气溶素受体以相同的方式锚定。这导致受体的选择性释放和啮齿动物细胞对气溶素的敏感性降低。人和牛的红细胞显示含有与大鼠红细胞受体具有相似性质的气溶素结合蛋白。具有GPI锚定的蛋白质被认为具有异常高的横向移动性，这可能是毒素如气溶素的优势，其在结合后必须寡聚化以成为插入感受态。
The plasma membrane of rat erythrocytes contains a 47-kDa glycoprotein that binds the channel-forming toxin aerolysin with high affinity and accounts for the sensitivity of these cells to the toxin. The receptor was purified so that its N-terminal sequence could be determined after Western blotting, The sequence did not match any sequences in the databases, indicating that the receptor is a novel erythrocyte surface protein, However, it exhibited considerable homology to the N-termini of a group of membrane proteins that are thought to be involved in ADP-ribosyl transfer reactions, A common property of these proteins is that they are attached to plasma membranes by C-terminal glycosylphosphatidylinositol (GPI) anchors. The aerolysin receptor was shown to be anchored in the same way by treating rat erythrocytes with phosphatidylinositol-specific phospholipase C. This caused the selective release of the receptor and a reduction in the rodent cells' sensitivity to aerolysin, Human and bovine erythrocytes were shown to contain an aerolysin-binding protein with similar properties to the rat erythrocyte receptor, Proteins with GPI anchors are thought to have unusually high lateral mobility, and this may be an advantage for a toxin, such as aerolysin, which must oligomerize after binding to become insertion competent.