The trypsin-like serine protease domain of Paralichthys olivaceus complement factor I regulates complement activation and inhibits bacterial growth
Autor: | Mo-fei Li, Cheng-dong Jin, Bei-bei Jia |
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Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
Flounder Complement factor I Aquatic Science law.invention Fish Diseases 03 medical and health sciences Downregulation and upregulation law Animals Environmental Chemistry Complement Activation Serine protease Bacteria biology Serine Endopeptidases 04 agricultural and veterinary sciences General Medicine biology.organism_classification Anti-Bacterial Agents Complement system Cell biology 030104 developmental biology Gene Expression Regulation Complement Factor I 040102 fisheries biology.protein Recombinant DNA 0401 agriculture forestry and fisheries iC3b Function (biology) Protein Binding |
Zdroj: | Fish & Shellfish Immunology. 97:18-26 |
ISSN: | 1050-4648 |
DOI: | 10.1016/j.fsi.2019.12.019 |
Popis: | 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. |
Databáze: | OpenAIRE |
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