Ujike Makoto, Taguchi Fumihiro
Laboratory of Virology and Viral Infections, Faculty of Veterinary Medicine, Nippon Veterinary and Life Science University, 1-7-1 Kyonan-cho, Musashino, Tokyo 180-8602, Japan.
Viruses. 2015 Apr 3;7(4):1700-25. doi: 10.3390/v7041700.
The envelopes of coronaviruses (CoVs) contain primarily three proteins; the two major glycoproteins spike (S) and membrane (M), and envelope (E), a non-glycosylated protein. Unlike other enveloped viruses, CoVs bud and assemble at the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). For efficient virion assembly, these proteins must be targeted to the budding site and to interact with each other or the ribonucleoprotein. Thus, the efficient incorporation of viral envelope proteins into CoV virions depends on protein trafficking and protein-protein interactions near the ERGIC. The goal of this review is to summarize recent findings on the mechanism of incorporation of the M and S glycoproteins into the CoV virion, focusing on protein trafficking and protein-protein interactions.
冠状病毒(CoVs)的包膜主要包含三种蛋白质;两种主要糖蛋白刺突(S)和膜(M),以及包膜(E),一种非糖基化蛋白。与其他包膜病毒不同,冠状病毒在内质网(ER)-高尔基体中间区室(ERGIC)出芽并组装。为了实现高效的病毒粒子组装,这些蛋白质必须靶向到出芽位点并相互作用或与核糖核蛋白相互作用。因此,病毒包膜蛋白有效整合到冠状病毒病毒粒子中取决于ERGIC附近的蛋白质运输和蛋白质-蛋白质相互作用。本综述的目的是总结关于M和S糖蛋白整合到冠状病毒病毒粒子机制的最新发现,重点关注蛋白质运输和蛋白质-蛋白质相互作用。