Analysis of a novel group of hydrophobic fungal proteins

Filamentous fungi need to adjust the surface properties of their hyphae to their environment to ensure the exploitation of new substrates and the survival of the fungal species. At hydrophobic/hydrophilic interfaces, such as air/water or the hydrophobic surface of living and non-living material in aqueous surroundings, fungi coat their hyphae with hydrophobic proteins to enable the formation of aerial hyphae or the adherence to surfaces. Hydrophobins, small amphipatic fungal proteins, are important key players during these processes and their functions are already relatively well understood. More recently a novel group of moderately hydrophobic proteins was described and named cerato-platanin family because the first member of this group was the protein cerato- platanin from the ascomycetous fungus Ceratocystis fimbriata. These proteins increasingly attracted attention in the fungal research area in the past few years. They were found to be abundantly expressed proteins under a variety of growth conditions, and they are also potent plant defence response elicitors. However, cerato-platanin proteins are present in the genomes of all ascomycetes and basidiomycetes, not only pathogens, and therefore their function in fungal growth still remains unclear. These proteins are an interesting novel target for further studies on the interaction of fungal hyphae with their environment at hydrophobic/hydrophilic interfaces and for analyzing the importance of these processes in fungal growth and development. Our aim in this project is to elucidate the function of proteins belonging to the novel cerato-platanin family in the biocontrol fungus Hypocrea atroviridis. We will study these novel proteins using a multidisciplinary approach of transcript analysis, gene knockouts, immunofluorescence and electron microscopy and biochemical characterization experiments. This project will contribute to significantly increase our understanding of how filamentous fungi interact with their environment, especially at hydrophobic/hydrophilic interfaces.