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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
Source PublicationFISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
Volume97Pages:18-26
Corresponding AuthorLi, Mo-fei(murphy210@163.com)
AbstractIn 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.
KeywordFactor I Complement Paralichthys olivaceus Antibacterial
DOI10.1016/j.fsi.2019.12.019
Indexed BySCI
Language英语
Funding ProjectNational 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 Research AreaFisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS SubjectFisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS IDWOS:000513983700003
PublisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/165512
Collection实验海洋生物学重点实验室
Corresponding AuthorLi, Mo-fei
Affiliation1.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
First Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Corresponding Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
GB/T 7714
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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