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<p>The retinoic acid-inducible gene I (RIG-I)-like receptors (RLRs) are major sensors against viral infection, but their roles in DNA virus infection largely remain unknown. This study found that a previously uncharacterised protein, pS183L, negatively regulates RLR signalling by suppressing MDA5 oligomerisation. Specifically, we showed that the overexpression of pS183L suppresses MDA5 but not cGAS-STING or RIG-I-induced IFN-β activation. Consistently, pS183L inhibited high molecular weight poly (I:C) activated IFN-β production. Furthermore, we demonstrated that pS183L interacts with CARDs and the MDA5 Helicase domain, consequently blocking MDA5 oligomerisation and the MDA5-MAVS interaction. Taken together, we concluded that pS183L blocks MDA5 oligomerisation through protein–protein interaction and thus disrupts MDA5-mediated IFN-β signalling.</p>

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ASFV pS183L protein negatively regulates RLR-mediated antiviral signalling by blocking MDA5 oligomerisation

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年3月31日

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  • Huan Chen,
  • Qun Yu,
  • Xiaoyu Gao,
  • Tao Huang,
  • Chenyi Bao,
  • Jiaona Guo,
  • Zhenzhong Wang,
  • Jiaxuan Lv,
  • Jianjun Dai,
  • Lorne A. Babiuk,
  • Xingqi Zou,
  • Yong-Sam Jung,
  • Yingjuan Qian

摘要

The retinoic acid-inducible gene I (RIG-I)-like receptors (RLRs) are major sensors against viral infection, but their roles in DNA virus infection largely remain unknown. This study found that a previously uncharacterised protein, pS183L, negatively regulates RLR signalling by suppressing MDA5 oligomerisation. Specifically, we showed that the overexpression of pS183L suppresses MDA5 but not cGAS-STING or RIG-I-induced IFN-β activation. Consistently, pS183L inhibited high molecular weight poly (I:C) activated IFN-β production. Furthermore, we demonstrated that pS183L interacts with CARDs and the MDA5 Helicase domain, consequently blocking MDA5 oligomerisation and the MDA5-MAVS interaction. Taken together, we concluded that pS183L blocks MDA5 oligomerisation through protein–protein interaction and thus disrupts MDA5-mediated IFN-β signalling.