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Purification and characterization of novel antifungal peptide, mouse beta defensin-1, in Escherichia coli

  1. Author:
    Wang, Y. L.
    Jiang, Y.
    Yang, D.
    Li, W. Y.
    Gong, T. X.
    Feng, Y.
    Jiang, Z. H.
    Li, M. Y.

  2. Author Address

    Li, Mingyuan] Sichuan Univ, State Key Lab Oral Dis, Chengdu 610041, Sichuan, Peoples R China. [Wang, Yueling, Jiang, Yan, Li, Wanyi, Gong, Tianxiang, Feng, Yan, Jiang, Zhonghua, Li, Mingyuan] Sichuan Univ, Dept Microbiol, W China Sch Preclin & Forens Med, Chengdu 610041, Peoples R China. [Yang, De] NCI, Basic Res Program, SAIC Frederick & Lab Mol Immunoregulat, NCI FCRDC,NIH, Frederick, MD 21702 USA.
    1. Year: 2009
  2. Journal: World Journal of Microbiology & Biotechnology
    1. 25
    2. 5
    3. Pages: 917-920
  4. Type of Article: Article
  1. Abstract:

    Mouse beta defensin-1 (mBD-1) is a cationic peptide with broad antimicrobial activity. The mBD-1 gene was cloned and fused with TrxA to construct pET32-mBD1, which was transformed into E. coli BL21 (DE3). The optimal expression conditions of fusion protein TrxA-mBD1 were: cultivation at 32A degrees C in 2 x YT medium, induction with 0.2 mM isopropylthio--galactoside (IPTG), and post-induction expression for 8 h. The fusion protein was highly soluble (90.0%) and accounted for 65% of the total soluble protein, and its volumetric productivity reached 0.67 g/l, i.e., 0.14 g/l of recombinant mBD-1. At 5 mu M, purified recombinant mBD-1 killed 50% of Candida albicans.

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  2. DOI: 10.1007/s11274-009-9956-y
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