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
中科院分区:
文献类型:
--
作者:
Omar OS;Simmons AJ;Andre NM;Wilson DW;Gross ST
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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