装配和出芽的流感病毒。
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Nayak DP、回族EK酒吧间招待员
装配和出芽的流感病毒。
病毒研究》2004年12月,106 (2):147 - 65。
- PubMed ID
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15567494 (在PubMed]
- 文摘
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流感病毒病原体的一种急性发热性呼吸道疾病被称为流感(俗称“流感”)和属于Orthomyxoviridae家庭。这些病毒具有分段,负链RNA基因组(vRNA)和包围,通常是球形和芽从质膜(更具体地说,顶端极化上皮细胞的质膜)。完整的病毒颗粒,因此,在感染细胞中是找不到的。病毒粒子包括三个主要subviral组件,即病毒囊膜、基质蛋白(M1),和核心(病毒ribonucleocapsid [vRNP])。周围的病毒包膜vRNP由脂质双分子层包含峰值由病毒糖蛋白(HA、NA和M2)外和内M1。病毒脂质,来自主机质膜,有选择地富含胆固醇和鞘糖脂。M1形成病毒信封和核心之间的桥梁。病毒核心由螺旋vRNP包含vRNA(负链)和NP以及少量的棉结和聚合酶复杂(PA、PB1和PB2)。发生病毒形态发生的,所有三个病毒成分,即病毒信封(含有脂质和跨膜蛋白),M1,并且vRNP必须带到大会网站,即极化上皮细胞顶端质膜。最后,必须形成芽在大会现场,与味蕾的关闭病毒粒子释放。 Transmembrane viral proteins are transported to the assembly site on the plasma membrane via the exocytic pathway. Both HA and NA possess apical sorting signals and use lipid rafts for cell surface transport and apical sorting. These lipid rafts are enriched in cholesterol, glycosphingolipids and are relatively resistant to neutral detergent extraction at low temperature. M1 is synthesized on free cytosolic polyribosomes. vRNPs are made inside the host nucleus and are exported into the cytoplasm through the nuclear pore with the help of M1 and NEP. How M1 and vRNPs are directed to the assembly site on the plasma membrane remains unclear. The likely possibilities are that they use a piggy-back mechanism on viral glycoproteins or cytoskeletal elements. Alternatively, they may possess apical determinants or diffuse to the assembly site, or a combination of these pathways. Interactions of M1 with M1, M1 with vRNP, and M1 with HA and NA facilitate concentration of viral components and exclusion of host proteins from the budding site. M1 interacts with the cytoplasmic tail (CT) and transmembrane domain (TMD) of glycoproteins, and thereby functions as a bridge between the viral envelope and vRNP. Lipid rafts function as microdomains for concentrating viral glycoproteins and may serve as a platform for virus budding. Virus bud formation requires membrane bending at the budding site. A combination of factors including concentration of and interaction among viral components, increased viscosity and asymmetry of the lipid bilayer of the lipid raft as well as pulling and pushing forces of viral and host components are likely to cause outward curvature of the plasma membrane at the assembly site leading to bud formation. Eventually, virus release requires completion of the bud due to fusion of the apposing membranes, leading to the closure of the bud, separation of the virus particle from the host plasma membrane and release of the virus particle into the extracellular environment. Among the viral components, M1 contains an L domain motif and plays a critical role in budding. Bud completion requires not only viral components but also host components. However, how host components facilitate bud completion remains unclear. In addition to bud completion, influenza virus requires NA to release virus particles from sialic acid residues on the cell surface and spread from cell to cell. Elucidation of both viral and host factors involved in viral morphogenesis and budding may lead to the development of drugs interfering with the steps of viral morphogenesis and in disease progression.