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<p>Cathepsin L (CTSL) as a cysteine cathepsin protease mediates complement C3 cleavage and pathogen degradation. In the present study, a CTSL homolog was identified from <i>Crassostrea gigas</i> (designated as <i>Cg</i>CTSL-2). Its mRNA expression increased significantly in hemocytes after <i>Vibrio splendidus</i> stimulation. The activity of r<i>Cg</i>CTSL-2 was induced after incubation with LPS or <i>V. splendidus</i> in Ca<sup>2+</sup>-dependent manner. r<i>Cg</i>CTSL-2 could specifically bound <i>V. splendidus</i> in Ca<sup>2+</sup>-dependent manner. The co-localization of r<i>Cg</i>CTSL-2 and <i>V. splendidus</i> was observed in cell-free hemolymph. Upon binding <i>V. splendidus</i>, <i>Cg</i>CTSL-2 interacted with <i>Cg</i>C3 in cell-free hemolymph and hemocytes. <i>Cg</i>C3 fragments in <i>Cg</i>CTSL-2-RNAi oysters and full length <i>Cg</i>C3 in r<i>Cg</i>CTSL-2-treated oysters were both reduced in cell-free hemolymph, respectively. <i>Cg</i>C3 fragments were accumulated in <i>Cg</i>CTSL-2-RNAi or r<i>Cg</i>CTSL-2-treated oysters. The co-localizations of <i>V. splendidus</i>, <i>Cg</i>C3, <i>Cg</i>CD18, <i>Cg</i>CTSL-2 and lysosomes were observed in hemocytes. These results suggested that <i>Cg</i>CTSL-2 upon binding <i>V. splendidus</i> directly interacted with <i>Cg</i>C3 to lead to <i>Cg</i>C3 cleavage and then <i>Cg</i>C3 fragments coated on <i>V. splendidus</i> were mediated by <i>Cg</i>CD18 into CTSL-2-lysosome pathway.</p>

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CTSL-2 upon specifically recognizing Vibrio splendidus directly cleaves complement C3 to promote the bacterial phagocytosis and degradation in oyster

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  • 发表日期：

    2025年4月24日

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  • Qiuyan Guo,
  • Wenwen Yang,
  • Weishuai Shan,
  • Hongsheng Yao,
  • Xiangqi Shi,
  • Lingling Wang,
  • Jiejie Sun,
  • Linsheng Song

摘要

Cathepsin L (CTSL) as a cysteine cathepsin protease mediates complement C3 cleavage and pathogen degradation. In the present study, a CTSL homolog was identified from Crassostrea gigas (designated as CgCTSL-2). Its mRNA expression increased significantly in hemocytes after Vibrio splendidus stimulation. The activity of rCgCTSL-2 was induced after incubation with LPS or V. splendidus in Ca2+-dependent manner. rCgCTSL-2 could specifically bound V. splendidus in Ca2+-dependent manner. The co-localization of rCgCTSL-2 and V. splendidus was observed in cell-free hemolymph. Upon binding V. splendidus, CgCTSL-2 interacted with CgC3 in cell-free hemolymph and hemocytes. CgC3 fragments in CgCTSL-2-RNAi oysters and full length CgC3 in rCgCTSL-2-treated oysters were both reduced in cell-free hemolymph, respectively. CgC3 fragments were accumulated in CgCTSL-2-RNAi or rCgCTSL-2-treated oysters. The co-localizations of V. splendidus, CgC3, CgCD18, CgCTSL-2 and lysosomes were observed in hemocytes. These results suggested that CgCTSL-2 upon binding V. splendidus directly interacted with CgC3 to lead to CgC3 cleavage and then CgC3 fragments coated on V. splendidus were mediated by CgCD18 into CTSL-2-lysosome pathway.