Involvement of clip-domain serine protease in the anti-Vibrio immune response of abalone (Haliotis discus hannai)- Molecular cloning, characterization and functional analysis
Involvement of clip-domain serine protease in the anti-Vibrio immune response of abalone (Haliotis discus hannai)- Molecular cloning, characterization and functional analysis
复制标题
夹域丝氨酸蛋白酶参与鲍鱼抗弧菌免疫反应 - 分子克隆、表征和功能分析
DOI:
10.1016/j.fsi.2017.10.062
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发表时间:
2018-01-01
影响因子:
4.7
通讯作者:
Cao, Min-Jie
中科院分区:
文献类型:
--
作者:
Hu, Jian-Jian;Chen, Yu-Lei;Cao, Min-Jie
Vibrio parahemolyticus (V. parahemolyticus) is a major pathogen for abalone, an important economical shellfish in coastal area of China. There is little known about the abalone innate immune system against pathogen infection. Clip-domain serine proteases (cSPs) are increasingly recognized to play important roles in host inunune defense in invertebrates. In this study, we cloned a cSP (Hdh-cSP) from abalone (Haliotis discus hannai). We found out that Hdh-cSP was widely expressed in multiple tissues of abalone, with highest level in the immune-like organ, hepatopancreas. V. parahemolyticus infection induced significantly elevated expression of Hdh-cSP in addition to better-characterized innate immune component genes including Rel/NF-kappa B, allograft inflammatory factor (ALInFa), macrophage expressed protein (MEP) and caspase-8. Importantly, the silencing of Hdh-cSP reduced the expression of these genes, suggesting that Hdh-cSP was an upstream regulatory factor in V. parahemolyticus infection. Further analysis showed that apoptosis of hemocytes was inhibited when the transcription of Hdh-cSP was knocked down, suggesting that Hdh-cSP participated in cell apoptosis by regulation of caspase 8 expression in V. parahemolyticus infection. Therefore, our study established an important role of cSP in the innate immunity against V. parahemolyticus infection in abalone.