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<p>In the present study, a new type of Caspase-1 homolog is identified from <i>Crassostrea gigas</i> (defined as <i>Cg</i>Cas1-2D). It is composed of 2×DSRM-CASc domain and has closer evolutionary relationship with mammalian Caspase-1s. The mRNA expressions of <i>Cg</i>Cas1-2D increase significantly after <i>Vibrio splendidus</i> or LPS stimulation. Recombinant <i>Cg</i>Cas1-2D and its 2×DSRM and CASc domains all bind various PAMPs and bacteria. r<i>Cg</i>Cas1-2D shows the highest binding activity to human Caspase-1 substrate. Upon recognizing bacteria, <i>Cg</i>Cas1-2D co-localizes and interacts with <i>Cg</i>GSDME, while it has no cleavage activity to <i>Cg</i>GSDME. <i>Cg</i>Cas1-2D inhibits the histone methylation and acetylation levels and <i>Cg</i>NF-κB/Rel nuclear translocation mediated by <i>Cg</i>GSDME. In addition, <i>Cg</i>Cas1-2D suppresses the mRNA expression levels of cytokines mediated by GSDME-NF-κB/Rel axis. The results demonstrate that a new type of anti-inflammatory Caspase-1 identified from oyster upon recognizing various bacteria interacts with GSDME to inhibit the histone modification and NF-κB signaling to suppress the inflammation.</p>

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A new type of Caspase-1 upon recognizing bacteria inhibits GSDME-dependent histone modification and NF-κB signaling

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年5月29日

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  • Renle Chang,
  • Jiejie Sun,
  • Jinyuan Leng,
  • Zihan Wang,
  • Shuyi Mu,
  • Yinan Li,
  • Jie Wang,
  • Linsheng Song

摘要

In the present study, a new type of Caspase-1 homolog is identified from Crassostrea gigas (defined as CgCas1-2D). It is composed of 2×DSRM-CASc domain and has closer evolutionary relationship with mammalian Caspase-1s. The mRNA expressions of CgCas1-2D increase significantly after Vibrio splendidus or LPS stimulation. Recombinant CgCas1-2D and its 2×DSRM and CASc domains all bind various PAMPs and bacteria. rCgCas1-2D shows the highest binding activity to human Caspase-1 substrate. Upon recognizing bacteria, CgCas1-2D co-localizes and interacts with CgGSDME, while it has no cleavage activity to CgGSDME. CgCas1-2D inhibits the histone methylation and acetylation levels and CgNF-κB/Rel nuclear translocation mediated by CgGSDME. In addition, CgCas1-2D suppresses the mRNA expression levels of cytokines mediated by GSDME-NF-κB/Rel axis. The results demonstrate that a new type of anti-inflammatory Caspase-1 identified from oyster upon recognizing various bacteria interacts with GSDME to inhibit the histone modification and NF-κB signaling to suppress the inflammation.