The saprophytic filamentous fungus Aspergillus fumigatus has been gaining importance as an opportunistic human pathogen over the past decades, as advances in modern medicine have created a growing group of patients susceptible to potentially deadly invasive aspergillosis. The role of fungal adhesion during infection progression is still poorly understood and this work aims to focus on this neglected aspect of the infection process. Fasciclin-like proteins can be found in a wide variety of organisms, where they often perform functions related to surface adhesion. Here we describe a fasciclin-like protein in A. fumigatus. The Fas protein was first discovered as differentially expressed in an O-mannosyltransferase Dpmt1 deletion strain, which indicates that it may be substantially glycosylated. We generated Dfas deletion strains in two different A. fumigatus strain backgrounds. The Dfas deletion strains grew normally on plates and in solution and neither bright field microscopy, nor TEM revealed phenotypical differences to the wildtype strains. Interestingly, the Dfas deletion strains showed reduced adhesion to hydrophobic plastic surfaces, but adhered normally to glass slides. Whether these altered adhesive properties have an effect on the strains’ virulence in mammalian hosts such as mice remains to be investigated.
Full conference title:
27th Fungal Genetics Conference
- FGC 27th (2013)