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<p>A common host response to pathogen infection involves the production of robust interferons or proinflammatory cytokines to activate the JAK-STAT pathway, thereby limiting pathogen replication. The bacterial pathogen <i>Legionella pneumophila</i> creates an intracellular niche and evades host immunity utilizing a cohort of effectors by diverse biochemical activities, thereby permissive for its intracellular replication. However, roles of the JAK-STAT pathway during bacterial infection remain elusive. Here, we identify for the first time that <i>L. pneumophila</i> acetyltransferase effector Lem17 acts as a negative regulator of the JAK-STAT signaling. Lem17 directly interacts with JAK1 through a JAK1-binding Box1-like motif, preventing its recruitment by cytokine receptors. As a YopJ-family acetyltransferase, Lem17 catalyzes Nε-lysine acetylation of JAK1 and impairs its kinase activity, thereby disrupting JAK1-mediated signaling transduction. Our findings provide insights into the mechanism by which <i>L. pneumophila</i> subverts host immunity through acetylation and underscore the role of the JAK-STAT pathway against bacterial infection.</p>

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A bacterial YopJ-family acetyltransferase suppresses host immune response by Nε-acetylation of JAK1

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月18日

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  • Tao-Tao Chen,
  • Si-Ru Zheng,
  • Binbin Yang,
  • Qiuhua Lu,
  • Xueyan Liu,
  • Wenhong Zhong,
  • Zhengfeng Jiang,
  • Fan Li,
  • Guosheng Hu,
  • Yue Feng,
  • Chunyi Hu,
  • Jingqian Su,
  • Songying Ouyang

摘要

A common host response to pathogen infection involves the production of robust interferons or proinflammatory cytokines to activate the JAK-STAT pathway, thereby limiting pathogen replication. The bacterial pathogen Legionella pneumophila creates an intracellular niche and evades host immunity utilizing a cohort of effectors by diverse biochemical activities, thereby permissive for its intracellular replication. However, roles of the JAK-STAT pathway during bacterial infection remain elusive. Here, we identify for the first time that L. pneumophila acetyltransferase effector Lem17 acts as a negative regulator of the JAK-STAT signaling. Lem17 directly interacts with JAK1 through a JAK1-binding Box1-like motif, preventing its recruitment by cytokine receptors. As a YopJ-family acetyltransferase, Lem17 catalyzes Nε-lysine acetylation of JAK1 and impairs its kinase activity, thereby disrupting JAK1-mediated signaling transduction. Our findings provide insights into the mechanism by which L. pneumophila subverts host immunity through acetylation and underscore the role of the JAK-STAT pathway against bacterial infection.