Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of hydrophobins are comprehensively discussed on the basis of recent findings. Multiple hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air-liquid interface, RolA of self-assembles via four stages, and its self-assembled films consist of two layers, a rodlet membrane facing air and rod-like structures facing liquid. The self-assembly depends mainly on hydrophobin conformation and solution pH. Cys4-Cys5 and Cys7-Cys8 loops, disulfide bonds, and conserved Cys residues of RodA-like hydrophobins are necessary for self-assembly at the interface and for adsorption to solid surfaces. AfRodA helps to evade recognition by the host immune system. RodA-like hydrophobins recruit cutinases to promote the hydrolysis of aliphatic polyesters. This mechanism appears to be conserved in and other filamentous fungi, and may be beneficial for their growth. Aspergilli produce various small secreted proteins (SSPs) including hydrophobins, hydrophobic surface-binding proteins, and effector proteins. Aspergilli may use a wide variety of SSPs to decompose solid polymers.