Characterization and function analysis of a Kazal-type serine proteinase inhibitor in the red claw crayfish Cherax quadricarinatus

doi:10.1016/j.dci.2020.103871

IOCAS-IR > 实验海洋生物学重点实验室

	Characterization and function analysis of a Kazal-type serine proteinase inhibitor in the red claw crayfish Cherax quadricarinatus
	Wang, Yan 1,3; Wang, Baojie 1; Liu, Mei 1; Jiang, Keyong 1; Wang, Mengqiang4,5,7 ; Wang, Lei 1,2,6
	2021
发表期刊	DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN	0145-305X
卷号	114 页码:10
通讯作者	Wang, Mengqiang([email protected]) ; Wang, Lei([email protected])
摘要	Kazal-type serine proteinase inhibitors (KPIs) function in physiological and immunological processes requiring pmteinase action. In the present study, the first Cherax quadricarinatus KPI gene (designated CqKPI) was identified and characterized. The open reading frame of CqKPI contains 405 nucleotides and encodes a protein of 134 amino acids. CqKPI has two Kazal domains comprising 44 amino acid residues with the conserved amino acid sequence C-X3-C-X-7-C-X-6-Y-X-3-C-X-6-C-X-12-C. Each Kazal domain has six conserved cysteine residues, which can form a structural conformation of three pairs of disulfide bonds stabilizing the Kazal domain. CqKPI exhibited high similarity with previously identified KPIs from crayfish hemocytes. The results of tissue distribution showed that CqKPI had the highest expression level in hemocytes, and this was in agreement with phylogenic relationships. Recombinant CqKPI (rCqKPI) was hetemlogously expressed in Escherichia coli and purified for further study. The proteinase inhibition assays suggested that rCqKPI could potently inhibit elastase and weakly inhibit trypsin, subtilisin A, and proteinase K, but not a-chymotrypsin. It can firmly bind to Bacillus hwajinpoensis, Staphylococcus aureus, and Vibrio parahaemolyticus, with weak binding to Candida albicans. In addition, CqKPI inhibited bacterial secretory pmteinase activity and inhibited the growth of B. hwajinpoensis and C. albicans. These data suggest that CqKPI might be involved in anti-bacterial immunity, acting as an inhibitor of the proteinase cascade in the resistance to invasion of pathogens.
关键词	Cherax quadricarinatus Kazal-type serine proteinase inhibitor Innate immunity
DOI	10.1016/j.dci.2020.103871
收录类别	SCI
语种	英语
资助项目	National Key R&D Program of China[2019YFD0900401]; STS program supporting project of Chinese Academy of Sciences of China[2019T3035]
WOS研究方向	Fisheries ; Immunology ; Zoology
WOS类目	Fisheries ; Immunology ; Zoology
WOS记录号	WOS:000588061100055
出版者	ELSEVIER SCI LTD
引用统计	被引频次：2[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/169106
专题	实验海洋生物学重点实验室
通讯作者	Wang, Mengqiang; Wang, Lei
作者单位	1.Chinese Acad Sci, Inst Oceanol, CAS Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Ocean Univ China, MOE Key Lab Marine Genet & Breeding, Qingdao 266003, Peoples R China 5.Ocean Univ China, Lab Trop Marine Germplasm Resources & Breeding En, SANYA Oceanog Inst, Sanya 572024, Peoples R China 6.Chinese Acad Sci, CAS Ctr Ocean Megasci, Qingdao 266400, Peoples R China 7.Natl Lab Marine Sci & Technol, Ctr Marine Mol Biotechnol, Qingdao 266237, Peoples R China
第一作者单位	中国科学院海洋研究所
通讯作者单位	中国科学院海洋研究所; 中国科学院海洋大科学研究中心
推荐引用方式 GB/T 7714	Wang, Yan,Wang, Baojie,Liu, Mei,et al. Characterization and function analysis of a Kazal-type serine proteinase inhibitor in the red claw crayfish Cherax quadricarinatus[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2021,114:10.
APA	Wang, Yan,Wang, Baojie,Liu, Mei,Jiang, Keyong,Wang, Mengqiang,&Wang, Lei.(2021).Characterization and function analysis of a Kazal-type serine proteinase inhibitor in the red claw crayfish Cherax quadricarinatus.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,114,10.
MLA	Wang, Yan,et al."Characterization and function analysis of a Kazal-type serine proteinase inhibitor in the red claw crayfish Cherax quadricarinatus".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 114(2021):10.

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