Division of Virology, Department of Microbiology and Immunology.
J Virol. 2013 Dec;87(23):12879-84. doi: 10.1128/JVI.02096-13. Epub 2013 Sep 25.
The influenza A virus possesses an eight-segmented, negative-sense, single-stranded RNA genome (vRNA). Each vRNA segment binds to multiple copies of viral nucleoproteins and a small number of heterotrimeric polymerase complexes to form a rod-like ribonucleoprotein complex (RNP), which is essential for the transcription and replication of the vRNAs. However, how the RNPs are organized within the progeny virion is not fully understood. Here, by focusing on polymerase complexes, we analyzed the fine structure of purified RNPs and their configuration within virions by using various electron microscopies (EM). We confirmed that the individual RNPs possess a single polymerase complex at one end of the rod-like structure and that, as determined using immune EM, some RNPs are incorporated into budding virions with their polymerase-binding ends at the budding tip, whereas others align with their polymerase-binding ends at the bottom of the virion. These data further our understanding of influenza virus virion morphogenesis.
甲型流感病毒拥有一个 8 节、负义、单链 RNA 基因组（vRNA）。每个 vRNA 片段与多个病毒核蛋白和少量异三聚体聚合酶复合物结合，形成棒状核糖核蛋白复合物（RNP），这对于 vRNA 的转录和复制是必不可少的。然而，子代病毒粒子中 RNP 是如何组织的还不完全清楚。在这里，我们通过聚焦于聚合酶复合物，使用各种电子显微镜（EM）分析了纯化的 RNP 的精细结构及其在病毒粒子中的构象。我们证实，每个 RNP 在棒状结构的一端都有一个单一的聚合酶复合物，并且通过免疫 EM 确定，一些 RNP 以其聚合酶结合端位于出芽尖端的方式被纳入正在出芽的病毒粒子中，而其他 RNP 则以其聚合酶结合端位于病毒粒子底部的方式排列。这些数据进一步加深了我们对流感病毒病毒粒子形态发生的理解。
