轮状病毒血凝素结构的三维可视化。
Three-dimensional visualization of the rotavirus hemagglutinin structure.
作者信息
Shaw A L, Rothnagel R, Chen D, Ramig R F, Chiu W, Prasad B V
机构信息
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
出版信息
Cell. 1993 Aug 27;74(4):693-701. doi: 10.1016/0092-8674(93)90516-s.
Abstract
Three-dimensional structures of a native simian and reassortant rotavirus have been determined by electron cryomicroscopy and computer image processing. The structural features of the native virus confirm that the hemagglutinin spike is a dimer of VP4, substantiated by in vivo radiolabeling studies. Exchange of native VP4 with a bovine strain equivalent results in a poorly infectious reassortant. No VP4 spikes are detected in the three-dimensional reconstruction of the reassortant. The difference map between the two structures reveals a novel large globular domain of VP4 buried within the virion that interacts extensively with the intermediate shell protein, VP6. Our results suggest that assembly of VP4 precedes that of VP7, the major outer shell protein, and that VP4 may play an important role in the receptor recognition and budding process through the rough endoplasmic reticulum during virus maturation.
摘要
通过电子冷冻显微镜和计算机图像处理技术，已确定了天然猿猴轮状病毒和重配轮状病毒的三维结构。天然病毒的结构特征证实，血凝素刺突是VP4的二聚体，体内放射性标记研究证实了这一点。用牛源等效株的天然VP4进行交换会产生感染性较差的重配病毒。在重配病毒的三维重建中未检测到VP4刺突。两种结构之间的差异图揭示了一个新的VP4大球状结构域，它埋在病毒粒子内，与中间壳蛋白VP6广泛相互作用。我们的结果表明，VP4的组装先于主要外壳蛋白VP7的组装，并且VP4可能在病毒成熟过程中通过粗糙内质网的受体识别和出芽过程中发挥重要作用。
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