UL13 protein, as a serine-threonine protein kinase of herpesvirus, is retained in the natural screening process and affects the life activities of the herpes virus. UL13 protein phosphorylates and modifies numerous cellular and viral proteins to affect the activation or inhibition of related protein functions and plays a variety of tasks during the life cycle of the herpes virus, such as immune escape and the establishment of a cell environment suitable for effective viral replication and virulence. How does UL13 hijack and utilize various cellular and viral proteins to achieve adequate immune clearance against the body and promote viral replication?

   The research progress was published in Frontiers In Immunology on 30 November 2022 under the title "Mechanism of herpesvirus protein kinase UL13 in immune escape and viral replication", DOI: 10.3389/fimmu.2022.1088690.

Figure 1, pUL13 inhibits the cGAS-STING signaling pathway and the NF-κB signaling pathway.