Stress- and Immunoproteomics

With the completion of fungal genome sequencing projects, it has become feasible to study gene and protein regulation in Aspergillus species and other fungi on a global scale. Several proteomic methods have been developed for the global profiling of protein levels in a cell at a given time, under defined conditions. Still, one of the most suitable protein separation techniques is based on 2D-gel electrophoresis, in which proteins are separated by charge and size in a gel matrix. Besides, LC-MS/MS-based proteomic methods have become more and more popular. Here, protein samples are extracted from cells, digested into peptides, then separated by liquid chromatography, ionised and transferred into a mass spectrometer. We are currently using both methods to:

  • investigate the proteome of the human-pathogenic fungus Aspergillus fumigatus. Our aim is to obtain a comprehensive overview about the proteins present during environmental changes, e. g. during stress conditions (hypoxia, oxidative stress, iron depletion, heat stress) or in the course of infection (interaction with phagocytes, interaction with bacteria).

2D-gels illustrating the differences in the protein expression profiles of A. fumigatus grown under low oxygen levels in comparison to control conditions. Green spots: increased protein levels under hypoxia, red spots: decreased protein levels under hypox

  • elucidate the proteins which trigger an immune response in healthy individuals and in patients with invasive mycoses by combining 2D-gel electrophoresis with immunoblotting
Workflow for the detection of immunoreactive A. fumigatus proteins
Workflow for the detection of immunoreactive A. fumigatus proteins
  • study the proteome of Aspergillus nidulans. Our special interest is the identification of target proteins of important transcription factors that are involved in the regulation of secondary metabolites and the characterization of regulatory circuits during stress adaptation.

  • elucidate the biological role of secreted proteins of the human-pathogenic dermatophyte Arthroderma benhamiae and the yeast Candida albicans.