病毒包膜糖蛋白在内质网中的折叠。
Folding of viral envelope glycoproteins in the endoplasmic reticulum.
作者信息
Braakman I, van Anken E
机构信息
Department of Bio-Organic Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands.
出版信息
Traffic. 2000 Jul;1(7):533-9. doi: 10.1034/j.1600-0854.2000.010702.x.
Abstract
Viral glycoproteins fold and oligomerize in the endoplasmic reticulum of the host cell. They employ the cellular machinery and receive assistance from cellular folding factors. During the folding process, they are retained in the compartment and their structural quality is checked by the quality control system of the endoplasmic reticulum. A special characteristic that distinguishes viral fusion proteins from most cellular proteins is the extensive conformational change they undergo during fusion of the viral and cellular membrane. Many viral proteins fold in conjunction with and dependent on a viral partner protein, sometimes even synthesized from the same mRNA. Relevant for folding is that viral glycoproteins from the same or related virus families may consist of overlapping sets of domain modules. The consequences of these features for viral protein folding are at the heart of this review.
摘要
病毒糖蛋白在宿主细胞的内质网中折叠并寡聚化。它们利用细胞机制并接受细胞折叠因子的协助。在折叠过程中，它们被保留在该区室中，其结构质量由内质网的质量控制系统进行检查。病毒融合蛋白与大多数细胞蛋白的一个特殊区别在于，它们在病毒膜与细胞膜融合过程中会经历广泛的构象变化。许多病毒蛋白与病毒伴侣蛋白一起折叠并依赖于该伴侣蛋白，有时甚至由同一mRNA合成。与折叠相关的是，来自相同或相关病毒家族的病毒糖蛋白可能由重叠的结构域模块集组成。这些特征对病毒蛋白折叠的影响是本综述的核心内容。
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