A novel C1qDC (PoC1qDC) with a collagen domain in Paralichthys olivaceus mediates complement activation and against bacterial infection. Issue 132 (January 2023)

• Record Type: Journal Article
• Authors: Li, Mo-fei; Zhang, Hong-qiang; Sun, Jin-sheng
• Is Part Of: Fish & shellfish immunology. Issue 132(2023)
• Publication Date: 2023-01
• Subjects: C1qDC -- Complement -- Paralichthys olivaceus -- Serum -- Bacterial infection; Fishes -- Immunology -- Periodicals; Shellfish -- Immunology -- Periodicals; Poissons -- Immunologie -- Périodiques; Crustacés -- Immunologie -- Périodiques; 571.9617
• DOI: 10.1016/j.fsi.2022.108472
• Languages: English
• ISSNs: 1050-4648

Abstract

Abstract: Complement C1q domain containing protein (C1qDC) is a vital recognition molecule and has an important effect on immunity. The C1qDCs exhibit opsonic activity in fish, while the mechanisms of C1qDCs in activation complement still remain unclear. This study explored immunological characteristics of a C1qDC from Japanese flounder ( Paralichthys olivaceus ) (PoC1qDC). PoC1qDC consists of 296 amino acid residues, possessing a collagen domain and a C1q domain. According to our results, PoC1qDC was expressed in 9 diverse tissue samples and showed up-regulation after bacterial challenge. Recombinant PoC1qDC (rPoC1qDC) activated normal serum bactericidal and hemolytic activities by interaction with Japanese flounder IgM, but not enhanced the complement activity of C3-depeleted serum. rPoC1qDC was significantly bound to various bacterial species and agglutination activity against Edwardsiella piscicida and Streptococcus iniae. Furthermore, rPoC1qDC showed direct interaction with peripheral blood leucocytes while enhancing phagocytic and chemotactic activity. When PoC1qDC was overexpressed in Japanese flounder before E. piscicida infection, bacterial replication was significantly inhibited in fish tissues. Consistently, when PoC1qDC expression in Japanese flounder was knocked down, bacterial replication was significantly enhanced. The above findings first suggested the role of PoC1qDC in teleost in mediating complement activation by interaction with IgM, which can positively influence bacterial infection. Highlights: PoC1qDC possesses a collagen domain and a C1q domain. Bacterial infection enhanced PoC1qDC expression in spleen, kidney and blood. Recombinant PoC1qDC mediated complement activation by interaction with IgM. Recombinant PoC1qDC could bind to bacteria and exhibited agglutination activity. PoC1qDC is required for optimal defense against bacterial infection.