Expression and functional characterization of a mannose-binding lectin-associated serine protease-1 (MASP-1) from Nile tilapia (Oreochromis niloticus) in host defense against bacterial infection. Issue 91 (August 2019)

• Record Type: Journal Article
• Authors: Mu, Liangliang; Yin, Xiaoxue; Wu, Hairong; Han, Kailiang; Wu, Liting; Ding, Mingmei; Bian, Xia; Li, Bingxi; Fu, Shengli; Liang, Fang; Guo, Zheng; Ye, Jianmin
• Is Part Of: Fish & shellfish immunology. Issue 91(2019)
• Page Start: 68
• Page End: 77
• Publication Date: 2019-08
• Subjects: Oreochromis niloticus -- MASP-1 -- Inflammation -- Streptococcus agalactiae -- Aeromonas hydrophila; Fishes -- Immunology -- Periodicals; Shellfish -- Immunology -- Periodicals; Poissons -- Immunologie -- Périodiques; Crustacés -- Immunologie -- Périodiques; 571.9617
• DOI: 10.1016/j.fsi.2019.05.014
• Languages: English
• ISSNs: 1050-4648

Abstract

Abstract: Mannose-binding lectin-associated serine protease-1 (MASP-1), a multifunctional serine protease, plays an important role in innate immunity which is capable of activating the lectin pathway of the complement system and also triggering coagulation cascade system. In this study, a MASP-1 homolog (OnMASP-1) was identified from Nile tilapia ( Oreochromis niloticus ) and characterized at expression and inflammation functional levels. The open reading frame (ORF) of OnMASP-1 is 2187 bp of nucleotide sequence encoding a polypeptide of 728 amino acids. The deduced amino acid sequence has 6 characteristic structures, including two C1r/C1s-Uegf-BMP domains (CUB), one epidermal growth factor domain (EGF), two complement control protein domains (CCP) and a catalytic serine protease domain (SP). Expression analysis revealed that the OnMASP-1 was highly expressed in the liver, and widely exhibited in other tissues containing intestine, spleen and kidney. In addition, the OnMASP-1 expression was significantly up-regulated in spleen and head kidney following challenges with Streptococcus agalactiae and Aeromonas hydrophila . The up-regulations of OnMASP-1 mRNA and protein expression were also demonstrated in hepatocytes and monocytes/macrophages in vitro stimulation with S. agalactiae and A. hydrophila . Recombinant OnMASP-1 protein was likely to participate in the regulation of inflammatory and migration reaction by monocytes/macrophages. These results indicated that OnMASP-1, playing an important role in innate immunity, was likely to involve in host defense against bacterial infection in Nile tilapia. Highlights: The MASP-1 gene was identified in Nile tilapia ( OnMASP-1 ). OnMASP-1 expression was significantly up-regulated following challenges with Streptococcus galactiae and Aeromonas hydrophila ( in vivo and in vitro ). Recombinant OnMASP-1 was likely to participate in the regulation of inflammatory and migration reaction.