LAUSR

Protein post-translational modifications (PTMs) are reversible processes that regulate the function of target proteins without altering their sequences. High-throughput sequencing surveys have provided insights into the patterns of PTMs, such as ubiquitination, SUMOylation, and phosphorylation. After primary infection, the Epstein-Barr virus (EBV), a ubiquitous herpesvirus, establishes a life-long latent infection. EBV can establish a delicate balance to regulate its proliferation and host cell survival. Owing to the limited gene products of EBV, interfering with the host PTM machinery is an effective way to alter host immune responses and physiological status and establish infection. In this review, we focus on the current knowledge of the mechanisms by which EBV products manipulate host ubiquitination, SUMOylation, and phosphorylation to establish a latent infection or favour viral replication and pathogenesis.