title: Recombinant medaka (Oryzias melastigmus) pro-hepcidin: Multifunctional characterization.
abstract: Recently, two hepcidin variant genes (Om-hep1 and Om-hep2) were identified in a model fish marine medaka and both were highly induced in vivo with bacterial challenge, suggesting that the medaka hepcidin may have a similar function to other reported teleostean hepcidins. In the present study, the antibacterial, antiviral and antitumor activities of Om-hep1 were determined using its synthetic and recombinant pro-peptides. The recombinant pro-hepcidin1 was expressed in Escherichia coli and an effective method to produce recombinant Pro-Omhep1 was developed in order to obtain a right folded structure. The results showed that both the synthetic mature peptide and recombinant pro-peptide had similar antibacterial activity against Gram-positive and negative bacteria. In particular, both the synthetic mature Om-hep1 and recombinant Pro-Omhep1 inhibited the viral replication of white spot syndrome virus in the hematopoietic tissue cells of the crayfish Cherax quadricarinatus. Om-hep1 also presented antitumor activity on the cultured human hepatocellular carcinoma cells. In addition, the antimicrobial mechanism of Om-hep1 was measured and it was found that Om-hep1 was likely to be non-membranolytic. The recombinant Pro-Omhep1 performed better biological activity compared to the synthetic mature Om-hep1. This study suggested that Om-hep1 was likely to be an important multifunction protein involved in various resistance actions in the marine medaka immune system.
authors: State Key Laboratory of Marine Environmental Science, College of Oceanography and Environmental Science, Xiamen University, Xiamen 361005, Fujian, China.
authors: Ling
authors: L
authors: Cai
authors: Jing-Jing
authors: JJ
authors: Cai
authors: Hai-Peng
authors: HP
authors: Liu
authors: Dan-Qing
authors: DQ
authors: Fan
authors: Hui
authors: H
authors: Peng
authors: Ke-Jian
authors: KJ
authors: Wang
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000302:isolation & purification / Q000494:pharmacology; D000906:Antibodies / Q000737:chemistry; D000918:Antibody Specificity; D023181:Antimicrobial Cationic Peptides / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology*; D000970:Antineoplastic Agents / Q000302:isolation & purification / Q000494:pharmacology; D000998:Antiviral Agents / Q000302:isolation & purification / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects; D015153:Blotting, Western; D002470:Cell Survival / Q000187:drug effects; D002478:Cells, Cultured; D002942:Circular Dichroism; D003001:Cloning, Molecular; D005393:Fish Diseases / Q000821:virology; D056945:Hep G2 Cells; D064451:Hepcidins; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D008826:Microbial Sensitivity Tests; D009990:Oryzias; D011487:Protein Conformation; D011498:Protein Precursors / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000494:pharmacology; D046848:White spot syndrome virus 1 / Q000187:drug effects
chemical_list: D000900:Anti-Bacterial Agents; D000906:Antibodies; D023181:Antimicrobial Cationic Peptides; D000970:Antineoplastic Agents; D000998:Antiviral Agents; C578702:HAMP protein, human; C579599:Hamp protein, mouse; D064451:Hepcidins; D011498:Protein Precursors; D011994:Recombinant Proteins