Structure and assembly of a paramyxovirus matrix protein
Structure and assembly of a paramyxovirus matrix protein
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DOI：
10.1073/pnas.1210275109
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发表时间：
2012-08-28
影响因子：
11.1
通讯作者：
Rossmann, Michael G.
中科院分区：
文献类型：
--
作者：
Battisti, Anthony J.;Meng, Geng;Rossmann, Michael G.
许多多形性脂质包膜病毒编码指导其组装和出芽的基质蛋白，但这一过程的机制尚不清楚。我们结合x射线晶体学和低温电子断层扫描显示，纽卡斯尔病病毒（麻疹病毒的一种副粘病毒和亲戚）的基质蛋白形成二聚体，组装成假四聚体阵列，产生病毒出芽所必需的膜曲率。我们发现糖蛋白锚定在基质蛋白之间的间隙中，螺旋核衣壳与基质阵列相关联。大约90%的病毒粒子缺乏基质阵列，这表明，与先前的生物学观察一致，基质蛋白在成熟过程中需要与病毒膜分离，这是核衣壳融合和释放到宿主细胞质中所必需的。结构和序列的保守性暗示其他副粘病毒基质蛋白的功能类似。
Many pleomorphic, lipid-enveloped viruses encode matrix proteins that direct their assembly and budding, but the mechanism of this process is unclear. We have combined X-ray crystallography and cryoelectron tomography to show that the matrix protein of Newcastle disease virus, a paramyxovirus and relative of measles virus, forms dimers that assemble into pseudotetrameric arrays that generate the membrane curvature necessary for virus budding. We show that the glycoproteins are anchored in the gaps between the matrix proteins and that the helical nucleocapsids are associated in register with the matrix arrays. About 90% of virions lack matrix arrays, suggesting that, in agreement with previous biological observations, the matrix protein needs to dissociate from the viral membrane during maturation, as is required for fusion and release of the nucleocapsid into the host's cytoplasm. Structure and sequence conservation imply that other paramyxovirus matrix proteins function similarly.