Bowden Thomas A, Crispin Max, Graham Stephen C, Harvey David J, Grimes Jonathan M, Jones E Yvonne, Stuart David I
University of Oxford, United Kingdom.
J Virol. 2009 Aug;83(16):8259-65. doi: 10.1128/JVI.00761-09. Epub 2009 Jun 3.
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.
引发严重出血热的新大陆沙粒病毒依靠其包膜糖蛋白附着并融合进入宿主细胞。在此,我们展示了马丘波病毒糖蛋白1(GP1)附着糖蛋白的晶体结构,该蛋白负责在细胞表面与转铁蛋白受体进行高亲和力结合。这种沙粒病毒糖蛋白的首个结构表明,GP1由一种新型的α/β折叠组成。这为新大陆沙粒病毒附着糖蛋白提供了蓝本,并揭示了一种利用起源不明的蛋白质折叠的病毒附着新结构。