The configuration of viral ribonucleoprotein complexes within the influenza A virion.
The configuration of viral ribonucleoprotein complexes within the influenza A virion.
复制标题
甲型流感病毒颗粒内病毒核糖核蛋白复合物的构型。
DOI：
10.1128/jvi.02096-13
复制
发表时间：
2013
影响因子：
5.4
通讯作者：
Hiroshi Sagara Takeshi Noda and Yoshihiro Kawaoka
中科院分区：
文献类型：
--
作者：
Yukihiko Sugita;Hiroshi Sagara Takeshi Noda and Yoshihiro Kawaoka
甲型流感病毒具有八节段、负义、单链RNA基因组（vRNA）。每个vRNA片段与病毒核蛋白的多个拷贝和少量异源三聚体聚合酶复合物结合，形成棒状核糖核蛋白复合物（RNP），其对于vRNA的转录和复制是必需的。然而，RNP如何在子代病毒体中组织尚不完全清楚。在这里，通过专注于聚合酶复合物，我们分析了纯化的RNP的精细结构和它们的配置内的病毒粒子，通过使用各种电子显微镜（EM）。我们证实，个别RNP拥有一个单一的聚合酶复合物在一端的棒状结构，并确定使用免疫EM，一些RNP被纳入到出芽病毒体与其聚合酶结合末端在出芽尖端，而其他对齐与其聚合酶结合末端在病毒体的底部。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。
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.