Identification and characterization of a cathepsin K homologue that interacts with pathogen bacteria in black rockfish, Sebastes schlegelii

文献类型： 外文期刊

第一作者： He, Shu-wen

作者： He, Shu-wen;Du, Xue;Wang, Guang-hua;Wang, Jing-jing;Xie, Bing;Gu, Qin-qin;Zhang, Min;Gu, Han-jie;Zhang, Min;Gu, Han-jie

作者机构：

关键词： Cathepsin K; Sebastes schlegelii; Bacterial infection; Immune defense

期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 影响因子：4.581； 五年影响因子：4.851 ）

ISSN： 1050-4648

年卷期： 2020 年 98 卷

页码：

收录情况： SCI

摘要： Cathepsin K belongs to the family of cysteine cathepsins. It is well known that the cysteine cathepsins participate in various physiological processes and host immune defense in mammals. However, in teleost fish, the function of cathepsin K is very limited. In the present study, a cathepsin K homologue (SsCTSK) from the teleost black rockfish (Sebastes schlegelii) was identified and examined at expression and functional levels. In silico analysis showed that three domains, including signal peptide, cathepsin propeptide inhibitor 129 domain, and functional domain Pept_C1, are existed in SsCTSK. SsCTSK also possesses a peptidase domain with three catalytically essential residues (Cys25, His162 and Asn183). Phylogenetic profiling indicated that SsCTSK was evolutionally close to the cathepsin K of other teleost fish. Expression of SsCTSK occurred in multiple tissues and was induced by bacterial infection. Purified recombinant SsCTSK (rSsCTSK) exhibited apparent maximal peptidase activity at 45 degrees C, and its enzymatic activity was remarkably declined in the presence of the cathepsin inhibitor E - 64. Moreover, rSsCTSK possesses the ability to bind with PAMPs and bacteria. Finally, knockdown of SsCTSK expression facilitated bacterial invasion in black rockfish. Collectively, these results indicated that SsCTSK functions as a cysteine protease and may serves as a target for pathogen manipulation of host defense system.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序