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Functional characterization of serine proteinase inhibitor Kazal-Type in the red claw crayfish Cherax quadricarinatus

文献类型： 外文期刊

作者： Shao, Shuoru 3 ; Liu, Kexin 3 ; Du, Jiansen 6 ; Yin, Chenlin 3 ; Wang, Mengqiang 3 ; Wang, Yan 1 ;

作者机构： 1.Chinese Acad Trop Agr Sci, Zhanjiang Expt Stn, Zhanjiang 524013, Peoples R China

2.Chinese Acad Trop Agr Sci, Sanya Res Inst, Sanya 572025, Peoples R China

3.Ocean Univ China, MOE Key Lab Marine Genet & Breeding, Qingdao 266003, Peoples R China

4.Ocean Univ China, Key Lab Trop Aquat Germplasm Hainan Prov Sanya Oce, Sanya 572024, Peoples R China

5.Hainan Yazhou Bay Seed Lab, Sanya 572024, Peoples R China

6.Qingdao Customs Dist PR China, Qingdao Int Travel Healthcare Ctr, Qingdao 266000, Peoples R China

关键词： Cherax quadricarinatus; Serine proteinase inhibitor kazal-type; Expression profiles; Bacteriostatic activity; Innate immunity

期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 影响因子：4.7； 五年影响因子：4.7 ）

ISSN： 1050-4648

年卷期： 2024 年 148 卷

页码：

收录情况： SCI

摘要： Serine protease inhibitors Kazal type (SPINKs) function in physiological and immunological processes across multicellular organisms. In the present study, we identified a SPINK gene, designated as CqSPINK, in the red claw crayfish Cherax quadricarinatus, which is the ortholog of human SPINK5. The deduced CqSPINK contains two Kazal domains consisting of 45 amino acid residues with a typical signature motif C-X3-C-X5-PVCG-X5-Y-X3-C-X6C-X12-14-C. Each Kazal domain contains six conserved cysteine residues forming three pairs of disulfide bonds, segmenting the structure into three rings. Phylogenetic analysis revealed CqSPINK as a homolog of human SPINK5. CqSPINK expression was detected exclusively in hepatopancreas and epithelium, with rapid upregulation in hepatopancreas upon Vibrio parahaemolyticus E1 challenge. Recombinant CqSPINK protein (rCqSPINK) was heterologously expressed in Escherichia coli and purified for further study. Proteinase inhibition assays demonstrated that rCqSPINK could potently inhibit proteinase K and subtilisin A, weakly inhibit alpha-chymotrypsin and elastase, but extremely weak inhibit trypsin. Furthermore, CqSPINK inhibited bacterial secretory proteinase activity from Bacillus subtilis, E. coli, and Staphylococcus aureus, and inhibited B. subtilis growth. These findings suggest CqSPINK's involvement in antibacterial immunity through direct inhibition of bacterial proteases, contributing to resistance against pathogen invasion.

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