PIAS1 potentiates the anti-EBV activity of SAMHD1 through SUMOylation

Abstract Background Sterile alpha motif and HD domain 1 (SAMHD1) is a deoxynucleotide triphosphohydrolase (dNTPase) that restricts the infection of variety RNA DNA viruses, including herpesviruses. The anti-viral function SAMHD1 associated with its dNTPase activity, which regulated by several post-translational modifications, phosphorylation, acetylation ubiquitination. Our recent studies also demonstrated E3 SUMO ligase PIAS1 functions as an Epstein-Barr virus (EBV) restriction factor. However, whether to restrict EBV replication remains unknown. Results In this study, we showed interacts promotes SUMOylation. We identified three lysine residues (K469, K595 K622) located on surface major SUMOylation sites. phosphorylated can be SUMOylated viral protein kinases. SUMOylation-deficient loses anti-EBV activity. Furthermore, genome in PIAS1-dependent manner. Conclusion study reveals synergizes inhibit lytic through protein–protein interaction