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The trypsin-like serine protease domain of Paralichthys olivaceus complement factor I regulates complement activation and inhibits bacterial growth
Jia, Bei-bei1,2,3; Jin, Cheng-dong1,2,3; Li, Mo-fei1,2
2020-02-01
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
卷号97页码:18-26
通讯作者Li, Mo-fei(murphy210@163.com)
摘要In mammals, complement factor I (CFI) is a serine protease in serum and plays a pivotal role in the regulation of complement activation. In the presence of cofactor, CFI cleaves C3b to iC3b, and further degrades iC3b to C3c and C3d. In teleost, the function of CFI is poorly understood. In this study, we examined the immunological property of CFI from Japanese flounder (Paralichthys olivaceus) (PoCFI), a teleost species with important economic value. PoCFI is composed of 597 amino acid residues and possesses a trypsin-like serine protease (Tryp) domain. We found that PoCFI expressions occurred in nine different tissues and were upregulated by bacterial challenge. Recombinant PoCFI-Tryp (rPoCFI-Tryp) inhibited complement activation and degraded C3b in serum. rPoCFI-Tryp exhibited apparent binding capacities to a board-spectrum of bacteria and inhibited bacterial growth. These results provide the first evidence to indicate that CFI in teleost negatively regulates complement activation via degradation C3b, and probably plays a role in host immune defense against bacterial infection.
关键词Factor I Complement Paralichthys olivaceus Antibacterial
DOI10.1016/j.fsi.2019.12.019
收录类别SCI
语种英语
资助项目National Natural Science Foundation of China[31972831] ; National Natural Science Foundation of China[31602197] ; Youth Innovation Promotion Association of the Chinese Academy of Sciences[2017249] ; Huiquan Young Scholar Program of Institute of Oceanology, CAS ; Taishan Scholar Program of Shandong Province
WOS研究方向Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS类目Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS记录号WOS:000513983700003
出版者ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
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被引频次:10[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/337002/165512
专题实验海洋生物学重点实验室
通讯作者Li, Mo-fei
作者单位1.Chinese Acad Sci, CAS Ctr Ocean Mega Sci, Inst Oceanol, CAS Key Lab Expt Marine Biol, Qingdao, Shandong, Peoples R China
2.Pilot Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Shandong, Peoples R China
3.Univ Chinese Acad Sci, Beijing, 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
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Jia, Bei-bei,Jin, Cheng-dong,Li, Mo-fei. The trypsin-like serine protease domain of Paralichthys olivaceus complement factor I regulates complement activation and inhibits bacterial growth[J]. FISH & SHELLFISH IMMUNOLOGY,2020,97:18-26.
APA Jia, Bei-bei,Jin, Cheng-dong,&Li, Mo-fei.(2020).The trypsin-like serine protease domain of Paralichthys olivaceus complement factor I regulates complement activation and inhibits bacterial growth.FISH & SHELLFISH IMMUNOLOGY,97,18-26.
MLA Jia, Bei-bei,et al."The trypsin-like serine protease domain of Paralichthys olivaceus complement factor I regulates complement activation and inhibits bacterial growth".FISH & SHELLFISH IMMUNOLOGY 97(2020):18-26.
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