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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >PUTATIVE RECEPTOR BINDING SITES ON ALPHAVIRUSES AS VISUALIZED BY CRYOELECTRON MICROSCOPY
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PUTATIVE RECEPTOR BINDING SITES ON ALPHAVIRUSES AS VISUALIZED BY CRYOELECTRON MICROSCOPY

机译:冷冻电子显微镜下可视化的对脂蛋白的受体结合位点

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The structures of Sindbis virus and Ross River virus complexed with Fab fragments from monoclonal antibodies have been determined from cryoelectron micrographs. Both antibodies chosen for this study bind to regions of the virions that have been implicated in cell-receptor recognition and recognize epitopes on the E2 glycoprotein. The two structures show that the Fab fragments bind to the outermost tip of the trimeric envelope spike protein. Hence, the same region of both the Sindbis virus and Ross River virus envelope spike is composed of E2 and is involved in recognition of the cellular receptor. [References: 49]
机译:从低温电子显微照片确定了与来自单克隆抗体的Fab片段复合的Sindbis病毒和Ross River病毒的结构。为这项研究选择的两种抗体都结合到与细胞受体识别有关的病毒体区域,并识别E2糖蛋白上的表位。这两个结构表明Fab片段结合至三聚体包膜刺突蛋白的最外端。因此,Sindbis病毒和Ross River病毒包膜刺的相同区域都由E2组成,并参与细胞受体的识别。 [参考:49]

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