Zhou Z H, Chen D H, Jakana J, Rixon F J, Chiu W
Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030, USA.
J Virol. 1999 Apr;73(4):3210-8. doi: 10.1128/JVI.73.4.3210-3218.1999.
Herpes simplex virus type 1 virions were examined by electron cryomicroscopy, allowing the three-dimensional structure of the infectious particle to be visualized for the first time. The capsid shell is identical to that of B-capsids purified from the host cell nucleus, with the exception of the penton channel, which is closed. The double-stranded DNA genome is organized as regularly spaced ( approximately 26 A) concentric layers inside the capsid. This pattern suggests a spool model for DNA packaging, similar to that for some bacteriophages. The bulk of the tegument is not icosahedrally ordered. However, a small portion appears as filamentous structures around the pentons, interacting extensively with the capsid. Their locations and interactions suggest possible roles for the tegument proteins in regulating DNA transport through the penton channel and binding to cellular transport proteins during viral infection.
通过电子冷冻显微镜对1型单纯疱疹病毒粒子进行了检查,首次使感染性粒子的三维结构得以可视化。衣壳外壳与从宿主细胞核中纯化的B型衣壳相同,但五聚体通道是关闭的。双链DNA基因组在衣壳内以规则间隔(约26埃)的同心层形式组织。这种模式表明了一种类似于某些噬菌体的DNA包装线轴模型。大部分包膜没有二十面体对称性。然而,一小部分表现为围绕五聚体的丝状结构,与衣壳广泛相互作用。它们的位置和相互作用表明包膜蛋白在病毒感染期间调节DNA通过五聚体通道运输以及与细胞运输蛋白结合方面可能发挥的作用。