Phosphorylated Eriocheir sinensis Rab10 regulates apoptosis and phagocytosis to defense Spiroplasma eriocheiris infection

文献类型： 外文期刊

第一作者： Ma, Yubo

作者： Ma, Yubo;Li, Qing;Wang, Xiaotong;Yan, Xinru;Li, Zhuoqing;Gu, Wei;Meng, Qingguo;Li, Qing;Ning, Mingxiao;Gu, Wei;Meng, Qingguo

作者机构：

关键词： Rab10; Phosphorylation; Spiroplasma eriocheiris; Apoptosis; Phagocytosis

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2025 年 306 卷

页码：

收录情况： SCI

摘要： The Rab GTPases play a crucial role in the regulation of immune responses towards viruses and bacteria infection in invertebrates. The proteomic data revealed Eriocheir sinensis Rab10 (EsRab10) phosphorylation was strongly decreased following Spiroplasma eriocheiris infection. However, the regulatory mechanism by which Rab10 modulates the innate immunity of E. sinensis against S. eriocheiris infection remains to be elucidated. In the present study, the coding sequence of EsRab10 identified as 609 bp, encoding a protein of 203 amino acids. EsRab10 was highly transcribed in diverse immune-related tissues of crab, including hepatopancreas, gills, and hemocytes, with a notable downregulation observed after S. eriocheiris infection. Knockdown of EsRab10 via RNA interference (RNAi) led to a significant increase in hemocyte apoptosis and a marked reduction in the phagocytic capacity of hemocytes against S. eriocheiris. Furthermore, EsRab10 RNAi resulted in an elevated S. eriocheiris load in hemocytes and a significant decrease in crab survival rates. Overexpression of EsRab10 in Drosophila Schneider 2 (S2) cells demonstrated that phosphorylation of EsRab10 enhanced cell viability, reduced apoptosis, increased phagocytic activity, and decreased the S. eriocheiris load in S2 cells. Conversely, dephosphorylation of EsRab10 exerted opposite effects. In summary, these results demonstrated that EsRab10 played a crucial role in the resistance of E. sinensis to S. eriocheiris infection by modulating apoptosis and phagocytosis through phosphorylation.

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