Leslie J, Rixon F J, McLauchlan J
MRC Virology Unit, Institute of Virology, Glasgow, Scotland.
Virology. 1996 Jun 1;220(1):60-8. doi: 10.1006/viro.1996.0286.
The tegument of herpes simplex virus type 1 (HSV-1) virus particles is a complex assemblage of virus proteins whose relative proportions within virions are essentially constant for a particular strain of virus. To examine the processes controlling incorporation into the tegument, we constructed a HSV-1 recombinant that expresses two copies of gene UL49, which encodes the major tegument protein VP22. One copy specifies the unmodified form of VP22 under the control of the native promoter while the second expresses an epitope-tagged version of the protein via the human cytomegalovirus immediate early promoter. In cells infected with the recombinant virus, the overall levels of VP22 synthesized were about fivefold higher than those for wild-type virus, due to the high levels of expression of tagged protein. Analysis of virus particles revealed that the amount of VP22 in the tegument was approximately two- to threefold higher in recombinant virions and L-particles than in particles produced by wild-type virus. These results provide the first evidence that, for certain proteins, the level of polypeptide synthesis can act as a controlling factor for the amount of protein incorporated into tegument.
1型单纯疱疹病毒（HSV-1）病毒颗粒的包膜是病毒蛋白的复杂组合，对于特定病毒株而言，其在病毒粒子中的相对比例基本恒定。为了研究控制包膜掺入的过程，我们构建了一种HSV-1重组体，它表达两份基因UL49，该基因编码主要包膜蛋白VP22。一份在天然启动子的控制下指定未修饰形式的VP22，而另一份通过人巨细胞病毒立即早期启动子表达该蛋白的表位标记版本。在感染重组病毒的细胞中，由于标记蛋白的高表达水平，合成的VP22总体水平比野生型病毒高出约五倍。对病毒粒子的分析表明，重组病毒粒子和L粒子包膜中VP22的含量比野生型病毒产生的粒子高出约两到三倍。这些结果首次证明，对于某些蛋白质，多肽合成水平可作为控制掺入包膜的蛋白量的一个因素。
