The projection structure of α-toxin from Staphylococcus aureus in human platelet membranes as analyzed by electron microscopy and image processing

A. Olofsson, U. Kavéus, M. Thelestam , H. Hebert
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引用次数: 20

Abstract

Most strains of Staphylococcus aureus produce α-toxin, a 33-kDa membrane active protein which is considered to be an important virulence factor of this bacterium. When α-toxin interacts with membranes an oligomeric form of the toxin can be seen by electron microscopy as characteristic ring structures in the membrane. A two-dimensional study of these annular structures, incorporated in membranes of human platelets, was performed, introducing a partly new method for rotational alignment of individual particles. It is shown that the averaged oligomer consists of six subunits. At neutral pH the outer diameter of the ring is about 75 Å. The stain-filled pore or cavity in the center has a diameter of about 25 Å. The size of the hexamer is increased if the pH is lowered.

用电子显微镜和图像处理分析金黄色葡萄球菌α毒素在人血小板膜中的投影结构
大多数金黄色葡萄球菌菌株产生α-毒素,一种33kDa的膜活性蛋白,被认为是该细菌的重要毒力因子。当α-毒素与膜相互作用时,通过电子显微镜可以看到寡聚形式的毒素是膜中的特征环结构。对这些结合在人类血小板膜中的环形结构进行了二维研究,引入了一种新的旋转排列单个颗粒的方法。结果表明,平均低聚物由六个亚基组成。在中性pH下,环的外径约为75Å。中心充满污渍的孔隙或空腔的直径约为25Å。如果pH降低,则六聚体的尺寸增大。
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