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The First Salamander Defensin Antimicrobial Peptide

Antimicrobial peptides have been widely identified from amphibian skins except salamanders. A novel antimicrobial peptide (CFBD) was isolated and characterized from skin secretions of the salamander, Cynops fudingensis. The cDNA encoding CFBD precursor was cloned from the skin cDNA library of C. fud...

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Autores principales: Meng, Ping, Yang, Shilong, Shen, Chuanbin, Jiang, Ke, Rong, Mingqiang, Lai, Ren
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3875428/
https://www.ncbi.nlm.nih.gov/pubmed/24386139
http://dx.doi.org/10.1371/journal.pone.0083044
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author Meng, Ping
Yang, Shilong
Shen, Chuanbin
Jiang, Ke
Rong, Mingqiang
Lai, Ren
author_facet Meng, Ping
Yang, Shilong
Shen, Chuanbin
Jiang, Ke
Rong, Mingqiang
Lai, Ren
author_sort Meng, Ping
collection PubMed
description Antimicrobial peptides have been widely identified from amphibian skins except salamanders. A novel antimicrobial peptide (CFBD) was isolated and characterized from skin secretions of the salamander, Cynops fudingensis. The cDNA encoding CFBD precursor was cloned from the skin cDNA library of C. fudingensis. The precursor was composed of three domains: signal peptide of 17 residues, mature peptide of 41 residues and intervening propeptide of 3 residues. There are six cysteines in the sequence of mature CFBD peptide, which possibly form three disulfide-bridges. CFBD showed antimicrobial activities against Staphylococcus aureus, Bacillus subtilis, Candida albicans and Escherichia coli. This peptide could be classified into family of β-defensin based on its seqeuence similarity with β-defensins from other vertebrates. Evolution analysis indicated that CFBD was close to fish β-defensin. As far as we know, CFBD is the first β-defensin antimicrobial peptide from salamanders.
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spelling pubmed-38754282014-01-02 The First Salamander Defensin Antimicrobial Peptide Meng, Ping Yang, Shilong Shen, Chuanbin Jiang, Ke Rong, Mingqiang Lai, Ren PLoS One Research Article Antimicrobial peptides have been widely identified from amphibian skins except salamanders. A novel antimicrobial peptide (CFBD) was isolated and characterized from skin secretions of the salamander, Cynops fudingensis. The cDNA encoding CFBD precursor was cloned from the skin cDNA library of C. fudingensis. The precursor was composed of three domains: signal peptide of 17 residues, mature peptide of 41 residues and intervening propeptide of 3 residues. There are six cysteines in the sequence of mature CFBD peptide, which possibly form three disulfide-bridges. CFBD showed antimicrobial activities against Staphylococcus aureus, Bacillus subtilis, Candida albicans and Escherichia coli. This peptide could be classified into family of β-defensin based on its seqeuence similarity with β-defensins from other vertebrates. Evolution analysis indicated that CFBD was close to fish β-defensin. As far as we know, CFBD is the first β-defensin antimicrobial peptide from salamanders. Public Library of Science 2013-12-30 /pmc/articles/PMC3875428/ /pubmed/24386139 http://dx.doi.org/10.1371/journal.pone.0083044 Text en © 2013 Rong et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Meng, Ping
Yang, Shilong
Shen, Chuanbin
Jiang, Ke
Rong, Mingqiang
Lai, Ren
The First Salamander Defensin Antimicrobial Peptide
title The First Salamander Defensin Antimicrobial Peptide
title_full The First Salamander Defensin Antimicrobial Peptide
title_fullStr The First Salamander Defensin Antimicrobial Peptide
title_full_unstemmed The First Salamander Defensin Antimicrobial Peptide
title_short The First Salamander Defensin Antimicrobial Peptide
title_sort first salamander defensin antimicrobial peptide
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3875428/
https://www.ncbi.nlm.nih.gov/pubmed/24386139
http://dx.doi.org/10.1371/journal.pone.0083044
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