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<p>The leucine rich repeat and sterile alpha motif containing 1 (LRSAM1) as E3 ligase recognizes bacteria and generates a ubiquitin signal to initiate the autophagy process. In the present study, LRSAM1 was identified from the Pacific oyster <i>Crassostrea gigas</i> (designed as <i>Cg</i>LRSAM1), which was able to recognize various pathogen-associated molecular patterns and bacteria and directly ubiquitinate <i>Vibrio splendidus. V. splendidus</i> was co-localized with <i>Cg</i>LRSAM1 and ubiquitin after invading haemocytes, and the ubiquitinated <i>V. splendidus</i> was then internalized into haemocyte lysosomes by p62-LC3-mediated autophagy. In haemocytes of <i>Cg</i>LRSAM1-RNAi oysters, the activation of <i>Cg</i>LC3 was enhanced after <i>V. splendidus</i> stimulation. While the co-localization values of <i>V. splendidus</i> with ubiquitin, <i>Cg</i>LC3 and lysosomes all decreased significantly after <i>V. splendidus</i> stimulation. These results indicated that <i>Cg</i>LRSAM1 functioned as E3 ligase responsible for anti-<i>Vibrio</i>-associated ubiquitination and regulated the degradation of bacteria through the ubiquitination-autophagy-lysosome pathway.</p>

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LRSAM1 mediated the degradation of intracellular Vibrio through the ubiquitination-autophagy-lysosome pathway in oyster

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  • 发表日期：

    2025年2月25日

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  • Wenwen Yang,
  • Jiejie Sun,
  • Qiuyan Guo,
  • Wei Wang,
  • Jinyuan Leng,
  • Lingling Wang,
  • Linsheng Song

摘要

The leucine rich repeat and sterile alpha motif containing 1 (LRSAM1) as E3 ligase recognizes bacteria and generates a ubiquitin signal to initiate the autophagy process. In the present study, LRSAM1 was identified from the Pacific oyster Crassostrea gigas (designed as CgLRSAM1), which was able to recognize various pathogen-associated molecular patterns and bacteria and directly ubiquitinate Vibrio splendidus. V. splendidus was co-localized with CgLRSAM1 and ubiquitin after invading haemocytes, and the ubiquitinated V. splendidus was then internalized into haemocyte lysosomes by p62-LC3-mediated autophagy. In haemocytes of CgLRSAM1-RNAi oysters, the activation of CgLC3 was enhanced after V. splendidus stimulation. While the co-localization values of V. splendidus with ubiquitin, CgLC3 and lysosomes all decreased significantly after V. splendidus stimulation. These results indicated that CgLRSAM1 functioned as E3 ligase responsible for anti-Vibrio-associated ubiquitination and regulated the degradation of bacteria through the ubiquitination-autophagy-lysosome pathway.