Rodriguez Boulan E, Pendergast M
Cell. 1980 May;20(1):45-54. doi: 10.1016/0092-8674(80)90233-0.
The surface distribution of the envelope glycoproteins of influenza, Sendai and Vesicular Stomatitis viruses was studied by immunofluorescence and immunoelectromicroscopy in infected epithelial cell monolayers, from which these viruses bud in a polarized fashion. It was found that before the onset of viral budding, the envelope proteins are exclusively localized into the same plasma membrane domains of the epithelial cells from which the virions ultimately bud: the glycoproteins of influenza and Sendai were detected at the apical surface, while the G protein of Vesicular Stomatitis virus was concentrated at the basolateral region. On the other hand, Sendai virus nucleocapsids, which can be easily identified in the cytoplasm before viral assembly, could be observed throughout the cell, not showing any preferential localization near the surface that the virions utilize for budding. These results are consistent with a model in which the asymmetric distribution of viral envelope proteins, rather than a polarized delivery of nucleocapsids, directs the polarity of viral budding. Furthermore, the asymmetric surface localization of viral glycoproteins suggests that these proteins share with intrinsic surface proteins of epithelial cells common biogenetic mechanisms and informational features or "sorting out" signals that determine their compartmentalization in the plasma membrane.
通过免疫荧光和免疫电子显微镜技术，对流感病毒、仙台病毒和水疱性口炎病毒包膜糖蛋白在感染的上皮细胞单层中的表面分布进行了研究，这些病毒以上皮细胞的极性方式出芽。研究发现，在病毒出芽开始之前，包膜蛋白仅定位在上皮细胞的同一质膜结构域中，病毒粒子最终从该结构域出芽：流感病毒和仙台病毒的糖蛋白在顶端表面被检测到，而水疱性口炎病毒的G蛋白则集中在基底外侧区域。另一方面，仙台病毒核衣壳在病毒组装前很容易在细胞质中识别，在整个细胞中都能观察到，在病毒粒子用于出芽的表面附近未显示出任何优先定位。这些结果与一个模型一致，在该模型中，病毒包膜蛋白的不对称分布而非核衣壳的极性运输决定了病毒出芽的极性。此外，病毒糖蛋白的不对称表面定位表明，这些蛋白与上皮细胞的内在表面蛋白具有共同的生物发生机制和信息特征或“分选”信号，这些信号决定了它们在质膜中的分隔。
