title: Molecular cloning, recombinant expression and antibacterial activity analysis of hepcidin from Simensis crocodile (Crocodylus siamensis).
abstract: Hepcidin, a cysteine-rich cationic antibacterial peptide, plays an important role in human defense against pathogen infection. However, its role in reptile immune response and whether it is involved in antibacterial immune have not yet been proven. In order to study the antibacterial activity of Crocodylus siamensis hepcidin (Cshepc), a common reptile which lives in topic region of Southeast Asia, a cDNA sequence of Cshepc was cloned, which included an open reading frame (ORF) of 300 bp encoding a 99 amino acid preprohepcidin. Cshepc has eight cysteines formed four conserved disulfide bridges, similarly to that of human's. Sequence analysis showed that Cshepc mature peptide was more conserved than that of preprohepcidin. Tissue expression analysis indicated that Cshepc transcripts were highly expressed in the liver, muscle and heart of C. siamensis. Recombinant expressed hepcidin could significantly inhibit the growth of the Gram-negative bacteria Escherichia coli and Aeromonas sobria as well as the Gram-positive bacterium Staphylococcus aureus, and Bacillus subtilis in vitro, suggesting that Cshepc, like human hepcidin could play a role in the antibacterial function in hosts innate immune response.
authors.affiliation: Key Laboratory for Aquatic Products Safety of Ministry of Education/State Key Laboratory of Biocontrol, The School of Life Sciences, Sun Yat-sen University, 135 Xingang West Street, Haizhu District, Guangzhou 510275, Guangdong Province, PR China.
authors.forename: Juan
authors.initials: J
authors.lastname: Hao
authors.forename: Yan-Wei
authors.initials: YW
authors.lastname: Li
authors.forename: Ming-Quan
authors.initials: MQ
authors.lastname: Xie
authors.forename: An-Xing
authors.initials: AX
authors.lastname: Li
mesh_terms: D000489:Alligators and Crocodiles / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D015870:Gene Expression; D064451:Hepcidins; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010843:Pichia / Q000235:genetics; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology*; D030162:Reptilian Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology*; D017421:Sequence Analysis
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; C578702:HAMP protein, human; C579599:Hamp protein, mouse; D064451:Hepcidins; D011994:Recombinant Proteins; D030162:Reptilian Proteins