An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: Evidence for reenvelopment during egress
An endoplasmic reticulum-retained herpes simplex virus glycoprotein H is absent from secreted virions: Evidence for reenvelopment during egress
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DOI：
10.1128/jvi.70.7.4311-4316.1996
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发表时间：
1996-07-01
影响因子：
5.4
通讯作者：
Wilson, DW
中科院分区：
文献类型：
--
作者：
Browne, H;Bell, S;Wilson, DW
尽管人们普遍认为疱疹病毒出口的第一步是核衣壳出芽进入核膜获得包膜，但该途径的后续事件尚未得到很好的理解。我们通过构建一种重组病毒，验证了病毒随后经历脱包膜的假设，随后在内质网（ER）外的膜上重新包膜，其中必需糖蛋白gH的表达通过内质网保留基序KKXX限制在内质网内核膜上。在重组病毒感染的细胞中，这一靶向信号赋予了预测的ER在gH上的定位特性，并且gH和gL多肽不能加工成成熟的形式，感染重组病毒的细胞释放的颗粒的感染性比感染野生型亲本病毒的细胞低100倍，但释放到培养基中的包膜病毒颗粒的数量没有改变。这些颗粒含有正常数量的go和VP16，但不含有可检测到的gH，这些数据与病毒退出模型一致，即细胞质中的裸核衣壳从亚细胞室获得最终包膜，而不是er内层核膜。
Although it is generally accepted that one of the first steps of herpesvirus egress is the acquisition of an envelope by nucleocapsids budding into the inner nuclear membrane, later events in the pathway are not well understood. We tested the hypothesis that the virus then undergoes de-envelopment, followed by reenvelopment at membranes outside the endoplasmic reticulum (ER), by constructing a recombinant virus in which the expression of an essential glycoprotein, gH, is restricted to the inner nuclear membrane-ER by means of the ER retention motif, KKXX. This targeting signal conferred the predicted ER localization properties on gH in recombinant virus-infected cells, and gH and gL polypeptides failed to become processed to their mature forms, Cells infected with the recombinant virus released particles with 100-fold less infectivity than those released by cells infected with the wild-type parent virus, yet the number of enveloped virus particles released into the medium was unaltered. These particles contained normal amounts of go and VP16 but did not contain detectable amounts of gH, and these data are consistent with a model of virus exit,whereby naked nucleocapsids in the cytoplasm acquire their final envelope from a subcellular compartment other than the ER-inner nuclear membrane.