Regulation of alphaherpesvirus protein via post-translational phosphorylation

Abstract

An alphaherpesvirus carries dozens of viral proteins in the envelope, tegument and capsid structure, and each protein plays an indispensable role in virus adsorption, invasion, uncoating and release. After infecting the host, a virus eliminates unfavourable factors via multiple mechanisms to escape or suppress the attack of the host immune system. Post-translational modification of proteins, especially phosphorylation, regulates changes in protein conformation and biological activity through a series of complex mechanisms. Many viruses have evolved mechanisms to leverage host phosphorylation systems to regulate viral protein activity and establish a suitable cellular environment for efficient viral replication and virulence. In this paper, viral protein kinases and the regulation of viral protein function mediated via the phosphorylation of alphaherpesvirus proteins are described. In addition, this paper provides new ideas for further research into the role played by the post-translational modification of viral proteins in the virus life cycle, which will be helpful for understanding the mechanisms of viral infection of a host and may lead to new directions of antiviral treatment.

Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field

“…Among substrates for protein kinases and protein phosphatases are proteins from both RNA and DNA viruses, and their phosphorylation forms an essential step in the viral life cycle [17][18][19][20][21][22]. Phosphorylation/dephosphorylation is mediated by cellular protein kinases/phosphatases, but some viruses encode their own protein kinases and protein phosphatases [23][24][25][26][27][28].…”