Journal
PATHOGENS
Volume 9, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/pathogens9110916
Keywords
US3; kinase; PRV; pseudorabies virus; alphaherpesvirus; phosphoproteome; mass spectrometry
Categories
Funding
- F.W.O.-Vlaanderen [G019617N, G060119N]
- Special Research Fund of Ghent University [GOA013-17, BAS003-18]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available