2. Academic Validation
  3. DDX56 cooperates with FMDV 3A to enhance FMDV replication by inhibiting the phosphorylation of IRF3

DDX56 cooperates with FMDV 3A to enhance FMDV replication by inhibiting the phosphorylation of IRF3

  • Cell Signal. 2019 Dec;64:109393. doi: 10.1016/j.cellsig.2019.109393.
Shao-Zu Fu 1,  Wen-Ping Yang 1,  Yi Ru 1,  Ke-Shan Zhang 1,  Yong Wang 1,  Xiang-Tao Liu 1,  Dan Li 2,  Hai-Xue Zheng 3
Affiliations

Affiliations

  • 1 State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, National Foot and Mouth Diseases Reference Laboratory, Chinese Academy of Agricultural Sciences, Lanzhou, China.
  • 2 State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, National Foot and Mouth Diseases Reference Laboratory, Chinese Academy of Agricultural Sciences, Lanzhou, China. Electronic address: lidan@caas.cn.
  • 3 State Key Laboratory of Veterinary Etiological Biology, Lanzhou Veterinary Research Institute, National Foot and Mouth Diseases Reference Laboratory, Chinese Academy of Agricultural Sciences, Lanzhou, China. Electronic address: haixuezheng@163.com.
PMID: 31445188 DOI: 10.1016/j.cellsig.2019.109393
Abstract

The components of foot-and-mouth disease virus (FMDV) interact with host cellular proteins to promote self-replication and evade the host immune response. Previous studies have shown that FMDV 3A, 2C and 2B proteins interact with host cellular proteins involved in FMDV replication. However, whether the Other host proteins have an impact on FMDV replication is less understood. In this study, we identified DDX56 as a positive regulator of FMDV replication. DDX56 overexpression increased FMDV replication, whereas DDX56 knockdown had the opposite effect. DDX56 interacted and cooperated with FMDV 3A to inhibit the type I interferon by reducing the phosphorylation of IRF3. Moreover, the D166 site of DDX56 played a role in increasing FMDV replication and cooperating with FMDV 3A to inhibit the phosphorylation of IRF3. Additionally, knockdown of DDX56 or FMDV 3A results also showed that DDX56 cooperated with FMDV 3A to inhibit the phosphorylation of IRF3. These results suggest that the interaction between FMDV 3A protein and the host protein DDX56 is critical for FMDV replication.

Keywords

DDX56; FMDV 3A; IRF3; Phosphorylation; Replication.

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