Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)

Background Hepcidins, a kind of cysteine-rich antimicrobial peptides, play important roles in host immunological processes and iron regulation, which have been identified from several fish species. The rare minnow (Gobiocypris rarus), an endemic cyprinid fish in China, has been used extensively as m...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Ke,Fei, Wang,Yun, Yang,Chuan-Shun, Xu,Chen
Lenguaje:	English
Publicado:	Pontificia Universidad Católica de Valparaíso 2015
Materias:	Cysteine residues Phylogenetic analysis Rare minnow hepcidin Synthetic peptide
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000300005
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:scielo:S0717-34582015000300005
record_format	dspace
spelling	oai:scielo:S0717-345820150003000052015-06-26Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)Ke,FeiWang,YunYang,Chuan-ShunXu,Chen Cysteine residues Phylogenetic analysis Rare minnow hepcidin Synthetic peptide Background Hepcidins, a kind of cysteine-rich antimicrobial peptides, play important roles in host immunological processes and iron regulation, which have been identified from several fish species. The rare minnow (Gobiocypris rarus), an endemic cyprinid fish in China, has been used extensively as model animal in laboratory. However, little is known about its hepcidin. Here, we report the cloning and characterization of a hepcidin gene from the liver of Chinese rare minnow. Results The full-length cDNA of rare minnow hepcidin is 662 bp, which contains an ORF of 273 bp encoding a prepropeptide of 90 amino acid residues. The predicted prepropeptide contains three domains: a signal peptide of 24 amino acids, a prodomain of 41 amino acids, and a mature peptide of 25 amino acids. Sequence alignment showed eight conserved cysteine residues in the mature peptide, which formed four disulfide bonds in spatial structure. The deduced structure of mature peptide showed a high degree of homology to the human hepcidin. Phylogenetic analysis showed that it had a close relationship with zebrafish hepcidin, and clustered in a clade with these from Cyprinidae. Synthetic peptide of rare minnow hepcidin could inhibit the growth of Gram positive bacterium Staphylococcus aureus and Gram negative bacteria Escherichia coli and Aeromonas hydrophila. Conclusion These results suggested that rare minnow hepcidin had typical structure of hepcidins and antibacterial activity. It could participate in innate immune response as an antibacterial agent and be used as antibiotic substance.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.18 n.3 20152015-05-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000300005en10.1016/j.ejbt.2015.03.003
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Cysteine residues Phylogenetic analysis Rare minnow hepcidin Synthetic peptide
spellingShingle	Cysteine residues Phylogenetic analysis Rare minnow hepcidin Synthetic peptide Ke,Fei Wang,Yun Yang,Chuan-Shun Xu,Chen Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)
description	Background Hepcidins, a kind of cysteine-rich antimicrobial peptides, play important roles in host immunological processes and iron regulation, which have been identified from several fish species. The rare minnow (Gobiocypris rarus), an endemic cyprinid fish in China, has been used extensively as model animal in laboratory. However, little is known about its hepcidin. Here, we report the cloning and characterization of a hepcidin gene from the liver of Chinese rare minnow. Results The full-length cDNA of rare minnow hepcidin is 662 bp, which contains an ORF of 273 bp encoding a prepropeptide of 90 amino acid residues. The predicted prepropeptide contains three domains: a signal peptide of 24 amino acids, a prodomain of 41 amino acids, and a mature peptide of 25 amino acids. Sequence alignment showed eight conserved cysteine residues in the mature peptide, which formed four disulfide bonds in spatial structure. The deduced structure of mature peptide showed a high degree of homology to the human hepcidin. Phylogenetic analysis showed that it had a close relationship with zebrafish hepcidin, and clustered in a clade with these from Cyprinidae. Synthetic peptide of rare minnow hepcidin could inhibit the growth of Gram positive bacterium Staphylococcus aureus and Gram negative bacteria Escherichia coli and Aeromonas hydrophila. Conclusion These results suggested that rare minnow hepcidin had typical structure of hepcidins and antibacterial activity. It could participate in innate immune response as an antibacterial agent and be used as antibiotic substance.
author	Ke,Fei Wang,Yun Yang,Chuan-Shun Xu,Chen
author_facet	Ke,Fei Wang,Yun Yang,Chuan-Shun Xu,Chen
author_sort	Ke,Fei
title	Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)
title_short	Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)
title_full	Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)
title_fullStr	Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)
title_full_unstemmed	Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)
title_sort	molecular cloning and antibacterial activity of hepcidin from chinese rare minnow (gobiocypris rarus)
publisher	Pontificia Universidad Católica de Valparaíso
publishDate	2015
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000300005
work_keys_str_mv	AT kefei molecularcloningandantibacterialactivityofhepcidinfromchineserareminnowgobiocyprisrarus AT wangyun molecularcloningandantibacterialactivityofhepcidinfromchineserareminnowgobiocyprisrarus AT yangchuanshun molecularcloningandantibacterialactivityofhepcidinfromchineserareminnowgobiocyprisrarus AT xuchen molecularcloningandantibacterialactivityofhepcidinfromchineserareminnowgobiocyprisrarus
_version_	1718441908127137792

Molecular cloning and antibacterial activity of hepcidin from Chinese rare minnow (Gobiocypris rarus)

Ejemplares similares