Non-ribosomal peptides play an important role in the virulence of the opportunistic pathogen Aspergillus fumigatus

Karen O'Hanlon[1] D. Stack[1] M. Schrettl[2] T. Larsen[3] K. Kavanagh[1] S. Doyle[1

Author address: 

1National Institute for Cellular Biotechnology, Department of Biology, National University of Ireland, Maynooth, Co. Kildare, Ireland, 2Division of Molecular Biology, Innsbruck Medical University, A-6020 Innsbruck, Austria 3Center for Microbial Biot


Aspergillus fumigatus is a ubiquitous filamentous fungus, and a serious opportunistic human pathogen. Availability of the complete genome sequence for A. fumigatus has revealed that there are at least eighteen genes coding for non-ribosomal peptide synthetases (NRPS). NRPS’s are usually large, multi-modular enzymes, comprised of discrete domains, which synthesise bioactive peptides via a thiotemplate mechanism. To date, a wide range of virulence factors have been reported for A. fumigatus, including adhesions, conidial pigments and proteases. Some of the best documented virulence factors for A. fumigatus include Gliotoxin and the iron-chelating Siderophores, which are of NRPS origin. Despite these important findings, there have been few studies relating the majority of A. fumigatus NRPS encoding genes to specific peptide products. This work aims to elucidate the peptide product encoded by a mono-modular NRPS, pesL (Afu6g12050/NRPS11), and to determine a possible role in virulence. A pesL deletion strain was generated, termed 8710;pesL. 8710;pesL displays severely reduced virulence in the Galleria mellonella model (p 1 mM) compared to the wild-type (p = 0.05), and severely increased susceptibility towards the antifungal voriconazole (> 0.25 µg/ml) compared to wild-type (p 0.5 µg/ml) compared to wild-type (p

abstract No: 


Full conference title: 

    • ECFG 10th (2010)