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    A nonribosomal peptide synthetase (Pes1) confers protection against oxidative stress in Aspergillus fumigatus


    Reeves, Emer P. and Reiber, Kathrin and Neville, Claire and Scheibner, Olaf and Kavanagh, Kevin and Doyle, Sean (2006) A nonribosomal peptide synthetase (Pes1) confers protection against oxidative stress in Aspergillus fumigatus. The FEBS Journal, 273 (13). pp. 3038-3053. ISSN 1742-464X

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    Abstract

    Aspergillus fumigatus is an important human fungal pathogen. The Aspergillus fumigatus genome contains 14 nonribosomal peptide synthetase genes, potentially responsible for generating metabolites that contribute to organismal virulence. Differential expression of the nonribosomal peptide synthetase gene, pes1, in four strains of Aspergillus fumigatus was observed. The pattern of pes1 expression differed from that of a putative siderophore synthetase gene, sidD, and so is unlikely to be involved in iron acquisition. The Pes1 protein (expected molecular mass 698 kDa) was partially purified and identified by immunoreactivity, peptide mass fingerprinting (36% sequence coverage) and MALDI LIFT-TOF ⁄TOF MS (four internal peptides sequenced). A pes1 disruption mutant (Dpes1) of Aspergillus fumigatus strain 293.1 was generated and confirmed by Southern and western analysis, in addition to RT-PCR. The Dpes1 mutant also showed significantly reduced virulence in the Galleria mellonella model system (P < 0.001) and increased sensitivity to oxidative stress (P ¼ 0.002) in culture and during neutrophil-mediated phagocytosis. In addition, the mutant exhibited altered conidial surface morphology and hydrophilicity, compared to Aspergillus fumigatus 293.1. It is concluded that pes1 contributes to improved fungal tolerance against oxidative stress, mediated by the conidial phenotype, during the infection process.

    Item Type: Article
    Additional Information: The definitive version is available at www.blackwell-synergy.com
    Keywords: chronic granulomatous disease; Galleria mellonella; nonrobosomal peptide synthetase; proteomics;
    Academic Unit: Faculty of Science and Engineering > Biology
    Faculty of Science and Engineering > Research Institutes > Institute of Immunology
    Item ID: 2174
    Identification Number: https://doi.org/10.1111/j.1742-4658.2006.05315.x
    Depositing User: Dr. Sean Doyle
    Date Deposited: 11 Oct 2010 11:51
    Journal or Publication Title: The FEBS Journal
    Publisher: Blackwell
    Refereed: Yes
    URI:

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