您好，欢迎访问中国热带农业科学院 机构知识库！
中国热带农业科学院机构知识库

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

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

作者： He, Shu-wen 1 ; Du, Xue 1 ; Wang, Guang-hua 1 ; Wang, Jing-jing 1 ; Xie, Bing 1 ; Gu, Qin-qin 1 ; Zhang, Min 1 ; Gu, Han- 1 ;

作者机构： 1.Qingdao Agr Univ, Marine Sci & Engn Coll, Qingdao 266109, Peoples R China

2.CATAS, Hainan Acad Trop Agr Resource, Inst Trop Biosci & Biotechnol, Haikou 571101, Hainan, Peoples R China

3.Pilot Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China

4.Hainan Prov Key Lab Funct Components Res & Utiliz, Haikou 571101, Hainan, Peoples R China

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.

  • 相关文献
作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：中国热带农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台