Pseudorabies virus and herpes simplex virus type 1 utilize different tegument-glycoprotein interactions to mediate the process of envelopment.

Pseudorabies virus and herpes simplex virus type 1 utilize different tegument-glycoprotein interactions to mediate the process of envelopment.
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DOI:
10.1159/000339467
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发表时间:
2013
期刊:
影响因子:
4.6
通讯作者:
Gross ST
Gross ST
中科院分区:
医学4区
文献类型:
--
作者:
Omar OS;Simmons AJ;Andre NM;Wilson DW;Gross ST

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在疱疹病毒衣壳化过程中,被膜多肽和膜蛋白在出芽位点组装,细胞脂质双层重新形成球形包膜。在这一过程中,被膜蛋白和病毒糖蛋白的胞质尾部之间的相互作用网络起着关键作用。我们先前已经证明,对于HSV-1,gH的胞质尾区结合被膜蛋白VP 16。HSV和PRV基因组基本上是共线的,并且单个基因产物显示出显著的序列同源性。然而,PRV和HSV蛋白之间的功能界限通常不同。本研究的目的是确定PRV gH和VP 16是否以类似于HSV中同源物的方式相互作用。进行融合蛋白下拉测定,其中将结合至谷胱甘肽-琼脂糖珠的PRV gH胞质尾-GST融合蛋白与PRV感染的细胞胞质溶胶一起孵育,洗涤,然后使用抗PRV VP 16抗血清进行Western印迹分析。Western印迹表明PRV VP 16不特异性结合PRV gH尾。我们的研究结果强调,尽管HSV和PRV之间的进化关系相对密切,但它们之间的蛋白质相互作用存在显着差异,从而推动了免疫。
During herpesvirus envelopment capsids, tegument polypeptides and membrane proteins assemble at the site of budding and a cellular lipid bilayer becomes refashioned into a spherical envelope. A web of interactions between tegument proteins and the cytoplasmic tails of viral glycoproteins play a critical role in this process. We have previously demonstrated that for HSV-1 the cytoplasmic tail of gH binds the tegument protein VP16. The HSV and PRV genomes are essentially collinear, and individual gene products show significant sequence homology. However the demarcation of function often differs between PRV and HSV proteins. The goal of this study was to determine whether PRV gH and VP16 interact in a manner similar to their homologs in HSV. A fusion protein pull-down assay was performed in which a PRV gH cytoplasmic tail-GST fusion protein, bound to Glutathione-Sepharose beads, was incubated with PRV-infected cell cytosol, washed, then subjected to Western blot analysis using anti-PRV VP16 antisera. Western blots indicate that PRV VP16 does not specifically bind to the PRV gH tail. Our results highlight that, despite the relatively close evolutionary relationship between HSV and PRV, there are significant differences in their protein interactions that drive envelopment.
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