期刊
PATHOGENS
卷 9, 期 11, 页码 -出版社
MDPI
DOI: 10.3390/pathogens9110916
关键词
US3; kinase; PRV; pseudorabies virus; alphaherpesvirus; phosphoproteome; mass spectrometry
类别
资金
- F.W.O.-Vlaanderen [G019617N, G060119N]
- Special Research Fund of Ghent University [GOA013-17, BAS003-18]
The US3 serine/threonine protein kinase is conserved among the alphaherpesvirus family and represents an important virulence factor. US3 plays a role in viral nuclear egress, induces dramatic alterations of the cytoskeleton, represses apoptosis, enhances gene expression and modulates the immune response. Although several substrates of US3 have been identified, an unbiased screen to identify US3 phosphorylation targets has not yet been described. Here, we perform a shotgun and phosphoproteomics analysis of cells expressing the US3 protein of pseudorabies virus (PRV) to identify US3 phosphorylation targets in an unbiased way. We identified several cellular proteins that are differentially phosphorylated upon US3 expression and validated the phosphorylation of lamin A/C at serine 404, both in US3-transfected and PRV-infected cells. These results provide new insights into the signaling network of the US3 protein kinase and may serve as a basis for future research into the role of the US3 protein in the viral replication cycle.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据