Molecular Characterisation and Phylogenetic Analysis of a Novel Isoform of Hepatic Antimicrobial Peptide, Hepcidin (Zc-hepc1), from the Coral Fish Moorish idol, Zanclus cornutus (Linnaeus, 1758)

• Published in: Probiotics and antimicrobial proteins 2013-09, Vol.5 (3), p.187-194
• Main Authors: Chaithanya, E. R, Philip, Rosamma, Sathyan, Naveen, Anil Kumar, P. R, Cubelio, Sherine Sonia, Bright Singh, I. S
• Format: Article
• Language: English
• Subjects: adenosine monophosphate; Applied Microbiology; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; cysteine; divergent evolution; fish; hepcidin; hydrophobicity; immune response; isoelectric point; Microbiology; molecular weight; Nutrition; phylogeny; Protein Science; signal peptide; Zanclus cornutus
• ISSN: 1867-1306; 1867-1314
• DOI: 10.1007/s12602-013-9139-x

Hepcidin is a family of short cysteine-rich antimicrobial peptides (AMPs) participating in various physiological functions with inevitable role in host immune responses. Present study deals with identification and characterisation of a novel hepcidin isoform from coral fish Zanclus cornutus. The 81 amino acid (aa) preprohepcidin obtained from Z. cornutus consists of a hydrophobic aa rich 22 mer signal peptide, a highly variable proregion of 35 aa and a bioactive mature peptide with 8 conserved cysteine residues which contribute to the disulphide back bone. The mature hepcidin, Zc-hepc1 has a theoretical isoelectric point of 7.46, a predicted molecular weight of 2.43 kDa and a net positive charge of +1. Phylogenetic analysis grouped Z. cornutus hepcidin with HAMP2 group hepcidins confirming the divergent evolution of hepcidin-like peptide in fishes. Zc-hepc1 can attain a β-hairpin-like structure with two antiparallel β-sheets. This is the first report of an AMP from the coral fish Z. cornutus.