Molecular characterisation and biological activity of an antiparasitic peptide from Sciaenops ocellatus and its immune response to Cryptocaryon irritans. (January 2022)

• Record Type: Journal Article
• Authors: Jin, Yuan; Mao, Yong; Niu, Su-Fang; Pan, Ying; Zheng, Wei-Hao; Wang, Jun
• Is Part Of: Molecular immunology. Volume 141(2022)
• Page Start: 1
• Page End: 12
• Publication Date: 2022-01
• Subjects: Cryptocaryon irritans -- Sciaenops ocellatus -- Novel piscidin-like -- Antiparasitic activity -- Immune response; Immunochemistry -- Periodicals; Molecular biology -- Periodicals; Immunochemistry -- Periodicals; Allergy and Immunology -- Periodicals; Molecular Biology -- Periodicals; Immunochimie -- Périodiques; Biologie moléculaire -- Périodiques; Immunochemistry; Molecular biology; Periodicals; Electronic journals; 571.96
• DOI: 10.1016/j.molimm.2021.08.010
• Languages: English
• ISSNs: 0161-5890

Abstract

Highlights: We identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus . So-pis is abound in glycine residues (22.7 %) and has a neutral isoelectric point. The synthetic peptide So-pis displayed weak haemolytic activity, limited or no activity against bacteria and fungi, but potent antiparasitic activity against C. irritans . So-pis might be involved in host defence against C. irritans infection. So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease. Abstract: Cryptocaryon irritans, a holotrichous ciliate parasitic protozoan, can trigger marine white spot disease and cause substantial economic losses in mariculture. However, methods of preventing and curing the disease have negatively affect fish, human, other organisms, and the natural environment. The antiparasitic activity of some antimicrobial peptides (AMPs) has garnered extensive attention of scholars. In this study, we identified and characterised a novel antiparasitic peptide, named So-pis, from Sciaenops ocellatus . The sequence analysis, structural features, and tissue distribution suggested that So-pis is genetically related to the piscidins family. However, So-pis showed a relatively low overall conservation compared with other known piscidins. So-pis is abound in glycine residues (22.7 %) and it has a neutral isoelectric point, weak amphipathicity, relatively long α-helix, and high hydrophobicity. These key elements are responsible for its biological activity. Quantitative real-time polymerase chain reaction (qRT-PCR) data indicated that So-pis is a typically gill-expressed peptide. The expression of So-pis in the gill, skin, spleen, and head kidney could be regulated during C. irritans infection, thereby implicating a role of So-pis in immune defence against C. irritans . The synthetic So-pis had limited or no antimicrobial activity against bacterial and yeasts but exhibited potent antiparasitic activity against C. irritans in vitro. The activity of synthetic So-pis against erythrocytes was less potent than its antiparasitic activity against C. irritans . These results indicated that So-pis might be one of the crucial defence cytokines against C. irritans in the red drum. Cumulatively, our data suggested that So-pis might be a potential candidate for developing a novel, effective, and safe therapeutic agent against marine white spot disease.