Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein
Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein
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DOI：
10.1128/jvi.00761-09
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发表时间：
2009-08-15
影响因子：
5.4
通讯作者：
Stuart, David I.
中科院分区：
文献类型：
--
作者：
Bowden, Thomas A.;Crispin, Max;Stuart, David I.
新世界沙粒病毒会引起严重的出血热，依赖其包膜糖蛋白附着并融合到宿主细胞中。在这里，我们展示了马丘波病毒 GP1 附着糖蛋白的晶体结构，该糖蛋白负责细胞表面与转铁蛋白受体的高亲和力结合。沙粒病毒糖蛋白的第一个结构表明 GP1 由新的 α/β 折叠组成。这提供了新世界沙粒病毒附着糖蛋白的蓝图，并揭示了使用来源未知的蛋白质折叠的病毒附着的新结构。
New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel alpha/beta fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown origins.