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通过电子显微镜和结晶学结合的Semliki森林病毒的目标膜插入的融合蛋白的可视化

Don L Gibbons¹, Inge Erk, Brigid Reilly

¹Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.

|September 19, 2003

概括

塞姆利基森林病毒使用其E1糖蛋白与宿主细胞融合. 这项研究可视化了插入细胞膜的E1同类三聚体 (E1HT),揭示了合作环结构.

科学领域:

病毒学病毒学
结构生物学结构生物学
细胞生物学细胞生物学

背景情况:

塞姆利基森林病毒 (SFV) 进入宿主细胞是通过受体介导的内细胞分裂开始的.
内体体内的低pH环境触发了膜融合,这是由病毒E1糖蛋白介导的过程.
在融合过程中,E1糖蛋白从E1/E2异构体发生显著的构造变化,变成稳定的E1同构体 (E1HT).

研究的目的:

在将其插入目标膜后,以结构性分析E1同类三聚体 (E1HT).
阐明由E1糖蛋白介导的病毒膜融合的机制.

主要方法:

使用电子冷显微镜 (cryo-EM) 来确定E1HT的3D结构.
2D晶体的电子晶体学提供了高分辨率的结构数据.
单质E1ectodomain的X射线结构被安装到3D重建中.

主要成果:

这项研究成功地可视化了插入脂质双层的E1同类三聚体 (E1HT),它代表了基膜中的病毒融合蛋白.
在插入后,E1域域垂直重新定向,域II的尖端嵌入到脂质双层中.
病毒融合蛋白的插入被观察到是一种合作过程,形成由五到六个E1同类三元体组成的环状结构.

结论:

这些发现提供了嵌入目标膜的病毒融合蛋白的详细可视化.
合作性,E1HT的环状组件表明了有效的病毒和宿主细胞膜融合的机制.

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