Bioinformatics analysis and characterization of a secretory cystatin fromThelohanellus kitauei

文献类型： 外文期刊

第一作者： Zhang, Fengli

作者： Zhang, Fengli;Gao, Chenchen;Yao, Yuanyuan;Xia, Rui;Hu, Juan;Zhou, Zhigang;Yang, Yalin;Ran, Chao;Zhang, Zhen

作者机构：

关键词： TK-cystatin; Thelohanellus kitauei; Bioinformatics analysis; Protease inhibitor; Inhibitory activity; Molecular docking

期刊名称：AMB EXPRESS （ 影响因子：3.298； 五年影响因子：3.427 ）

ISSN： 2191-0855

年卷期： 2020 年 10 卷 1 期

页码：

收录情况： SCI

摘要： Thelohanellus kitauei, is a member of obligate parasitic myxozoans, which causes intestinal giant-cystic disease of common carp (Cyprinus carpio) and has resulted in significant economic losses in carp farms. Cystatin secreted by parasites can regulate the immune response of host to facilitate parasite's survival. In this study, the secretory TK-cystatin gene, encoding a protein of 120 amino acid residues (13.65 kDa), was cloned fromT. kitaueigenome. Phylogenetic analysis showed that TK-cystatin gene is closely related to the cystatin-A fromHydra vulgaris. Multiple sequence alignment revealed that TK-cystatin had three conserved motifs: N-terminal G(19)G(20), Q(73)VVAG(77), and C-terminal (LP103)-P-102. Molecular docking between TK-cystatin and three cysteine proteases showed a lower binding energy (- 13 KJ/mol) with cathepsin L whereas a higher binding energy (- 8.6 KJ/mol) with cathepsin B. TK-cystatin gene was expressed inEscherichia coli. Activity assays revealed that TK-cystatin has stronger inhibitory activity on endopeptidases (papain and cathepsin L) and weaker inhibitory activity on exopeptidase (cathepsin B). TK-cystatin was stable under the condition of acidity or alkalinity or below 57 degrees C. This study laid a foundation for the design and development of the anti-T. kitaueivaccine in carp culture in the future.

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