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Two novel antimicrobial peptides from skin secretions of the frog, Rana nigrovittata

Authors

  • Xiuhong Liu,

    1. Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China
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    • Both authors contributed equally to this paper.

  • Rui Liu,

    1. Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China
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    • Both authors contributed equally to this paper.

  • Lin Wei,

    1. Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China
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  • Hailong Yang,

    1. Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China
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  • Keyun Zhang,

    1. Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China
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  • Jingze Liu,

    Corresponding author
    1. College of Life Sciences School of Hebei Normal University, Shijiazhuang, Hebei 050016, China
    • College of Life Sciences School of Hebei Normal University, Shijiazhuang, Hebei 050016, China.
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  • Ren Lai

    Corresponding author
    1. Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China
    2. Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China
    • Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
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Abstract

Two novel antimicrobial peptides with similarity to brevinin-2 family are purified and characterized from the skin secretions of the frog, Rana nigrovittata. Their amino acid sequences were determined as GAFGNFLKGVAKKAGLKILSIAQCKLSGTC (brevinin-2-RN1) and GAFGNFLKGVAKKAGLKILSIAQCKLFGTC (brevinin-2-RN2), respectively, by Edman degradation. Different from brevinin-2, which is composed of 33 amino acid residues (aa), both brevinin-2-RN1 and -RN2 contain 30 aa. Five cDNA sequences (Genbank accession numbers, EU136465-9) encoding precursors of brevinin-2-RN1 and -RN2 were screened from the skin cDNA library of R. nigrovittata. These precursors are composed of 72 aa including a predicted signal peptide, an acidic spacer peptide, and a mature brevinin-2-RN. Both brevinin-2-RN1 and -RN2 showed strong antimicrobial activities against gram-positive and gram-negative bacteria and fungi. The current work identified and characterized two novel antimicrobial peptides with unique primary structure. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.

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