Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm
Herpes simplex virus glycoproteins gD and gE/gI serve essential but redundant functions during acquisition of the virion envelope in the cytoplasm
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DOI：
10.1128/jvi.77.15.8481-8494.2003
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发表时间：
2003-08-01
影响因子：
5.4
通讯作者：
Johnson, DC
中科院分区：
文献类型：
--
作者：
Farnsworth, A;Goldsmith, K;Johnson, DC
单纯疱疹病毒（HSV）和其他疱疹病毒的后期组装尚不清楚。最终病毒粒子包膜的获得显然涉及被膜蛋白包裹的病毒核衣壳和膜糖蛋白的细胞质结构域之间的相互作用。这促进病毒颗粒出芽进入由反式高尔基网络或核内体产生的细胞质囊泡。参与这些过程的病毒膜糖蛋白和被膜蛋白的特性尚不清楚。在这里，我们报道了HSV突变体缺乏两种病毒糖蛋白，gD和gE，在细胞质中积累了大量未包膜的核衣壳。这些聚集的衣壳浸泡在一个电子密集的层中，看起来像是被皮。很少或未观察到包膜病毒粒子。在不能表达gD和gI的HSV中观察到更细微的缺陷。缺乏gD、gE和gI的三突变体在包膜上表现出更严重的缺陷。我们得出结论，HSV gD和gE/gI异二聚体复合物以冗余方式将病毒粒子包膜锚定在被膜衣壳上。在缺乏这两种HSV糖蛋白中的任何一种情况下，包膜继续进行；然而，没有gD和gE，或gE/gI，细胞质包膜受到严重抑制。
The late stages of assembly of herpes simplex virus (HSV) and other herpesviruses are not well understood. Acquisition of the final virion envelope apparently involves interactions between viral nucleocapsids coated with tegument proteins and the cytoplasmic domains of membrane glycoproteins. This promotes budding of virus particles into cytoplasmic vesicles derived from the trans-Golgi network or endosomes. The identities of viral membrane glycoproteins and tegument proteins involved in these processes are not well known. Here, we report that HSV mutants lacking two viral glycoproteins, gD and gE, accumulated large numbers of unenveloped nucleocapsids in the cytoplasm. These aggregated capsids were immersed in an electron-dense layer that appeared to be tegument. Few or no enveloped virions were observed. More subtle defects were observed with an HSV unable to express gD and gI. A triple mutant lacking gD, gE, and gI exhibited more severe defects in envelopment. We concluded that HSV gD and the gE/gI heterodimeric complex act in a redundant fashion to anchor the virion envelope onto tegument-coated capsids. In the absence of either one of these HSV glycoproteins, envelopment proceeds; however, without both gD and gE, or gE/gI, there is profound inhibition of cytoplasmic envelopment.