病毒组装与释放
中文名称
通路描述
SARS 病毒在 ERGIC 膜上组装（参见 Masters, 2006; Fehr and Perlman, 2015; Fung and Liu, 2019）。病毒膜蛋白组分在 ERGIC 膜上浓缩，但也存在于分泌系统中，包括细胞膜。病毒组装部位的积累依赖于细胞质尾部中的检索信号与宿主因子（如 COPI 包被）之间的相互作用，并可能涉及反复的顺行和逆行运输（McBride et al, 2007; Ujike et al, 2016; Tan et al, 2004; Tan et al, 2005; 参见 McBride and Fielding, 2012; Chang et al, 2014）。病毒组装由 M 蛋白的同型相互作用启动（Tseng et al, 2010; Siu et al, 2008）。这形成一个 M 晶格，有助于诱导膜弯曲，并作为招募病毒其他结构组分的支架（Voss et al, 2009）。M 蛋白与成熟病毒的主要组分（E、S 和 N）相互作用（He et al, 2004; Luo et al, 2006; Siu et al, 2008; 参见 Masters, 2006）。电子显微镜研究表明成熟病毒的大小约为 100 nm。核糖核蛋白颗粒主要是螺旋状，直径约为 16 nm（Neuman et al, 2006; Neuman et al, 2011; 参见 Chang et al, 2014）。这些物理限制表明成熟病毒中 75 S 三聚体：1200 M 蛋白：300 N：1 个 RNA 基因组的比例（Neuman et al, 2011; 参见 Chang et al, 2014）。其他病毒蛋白（包括 E、3a 和 7a）以少量存在，可能是成熟病毒组分，但其功能尚未完全确定（参见 Schoeman and Fielding, 2019; Liu et al, 2014）。
英文描述
Virion Assembly and Release SARS viral assembly occurs at the ERGIC membrane (reviewed in Masters, 2006; Fehr and Perlman, 2015; Fung and Liu, 2019). Membrane protein components of the virus concentrate at the ERGIC membrane but are also found throughout the secretory system including at the plasma membrane. Accumulation at the site of viral assembly has been shown to depend on interaction between retrieval signals in the cytoplasmic tails of viral proteins and host factors such as the COPI coat, and likely involves repeated rounds of anterograde and retrograde traffic (McBride et al, 2007; Ujike et al, 2016; Tan et al, 2004; Tan et al, 2005; reviewed in McBride and Fielding, 2012; Chang et al, 2014).
Viral assembly is intitiated by homotypic interactions of M protein (Tseng et al, 2010; Siu et al, 2008). This forms an M-lattice that contributes to the induction of membrane curvature and additionally acts as a scaffold for the recruitment of the other structural components of the virus (Voss et al, 2009). M protein makes interactions with each of the main components of the mature virus, including E, S and N (He et al, 2004; Luo et al, 2006; Siu et al, 2008; reviewed in Masters, 2006). Electron micrographic studies suggest the final size of the mature virus is ~100 nm. The ribonuclear particle is predominantly helical and is packaged with an outer diamter of ~ 16 nm (Neuman et al, 2006; Neuman et al, 2011; reviewed in Chang et al, 2014). These physical constraints suggest a final stoichiometry in the mature virion of 75 S trimers:1200 M proteins:300 N:1 RNA genome (Neuman et al, 2011; reviewed in Chang et al, 2014). Minor amounts of other viral proteins, including proteins E, 3a and 7a may also be components of the mature virus, although their functions are not well established (reviewed in Schoeman and Fielding, 2019; Liu et al, 2014).
Viral assembly is intitiated by homotypic interactions of M protein (Tseng et al, 2010; Siu et al, 2008). This forms an M-lattice that contributes to the induction of membrane curvature and additionally acts as a scaffold for the recruitment of the other structural components of the virus (Voss et al, 2009). M protein makes interactions with each of the main components of the mature virus, including E, S and N (He et al, 2004; Luo et al, 2006; Siu et al, 2008; reviewed in Masters, 2006). Electron micrographic studies suggest the final size of the mature virus is ~100 nm. The ribonuclear particle is predominantly helical and is packaged with an outer diamter of ~ 16 nm (Neuman et al, 2006; Neuman et al, 2011; reviewed in Chang et al, 2014). These physical constraints suggest a final stoichiometry in the mature virion of 75 S trimers:1200 M proteins:300 N:1 RNA genome (Neuman et al, 2011; reviewed in Chang et al, 2014). Minor amounts of other viral proteins, including proteins E, 3a and 7a may also be components of the mature virus, although their functions are not well established (reviewed in Schoeman and Fielding, 2019; Liu et al, 2014).
所含基因
1 个基因