Characterization, Expression, and Functional Analysis of the Northern Snakehead (Channa argus) Hepcidin.

Abstract

Hepcidin, an antimicrobial peptide (AMP), is a well-conserved molecule present in various species such as fish, amphibians, birds, reptiles, and mammals. It exhibits broad-spectrum antimicrobial activity and holds a significant role in the innate immune system of host organisms. The northern snakehead (Channa argus) has become a valuable freshwater fish in China and Asia. In this investigation, the cDNA encoding the hepcidin gene of northern snakehead was cloned and named caHep. The amino acid sequences and protein structure of caHep are similar to those of hepcidins from other fish. The eukaryotic expression product of the caHep gene showed broad-spectrum antibacterial activity. Scanning electron microscope analysis indicated that the caHep peptide inhibited bacterial growth by damaging their cell membranes. Lipopolysaccharide (LPS) injection induced significant expression of caHep, implying the involvement of caHep in the innate immune response of northern snakeheads. This investigation showed that the caHep peptide is potentially a robust antibacterial drug against bacterial diseases in aquaculture animals.