Aspergillus fumigatus hydrophobin functional amyloids

Long-time perceived as aberrant conformations associated to disease, it is now established that proteins can adopt the amyloid fold to perform their function. Hydrophobins are fungal proteins characterized by a conserved amphipathic profile and an idiosyncratic pattern of cysteine residues involved in four disulfide bridges. Their functions are due to their remarkable physicochemical properties. These proteins are secreted in a soluble form that self-assembles at hydrophobic/hydrophilic or air/water interfaces to form amphipathic layers consisting of protein amyloids with a rodlet morphology.