Class I hydrophobins function in fungal growth and development by self-assembling at hydrophobic-hydrophilic interfaces into amyloid-like fibrils. SC3 of the mushroom forming fungus Schizophyllum commune is the best studied class I hydrophobin. This protein spontaneously adopts the amyloid state at the water-air interface. In contrast, SC3 is arrested in an intermediate conformation at the interface between water and a hydrophobic solid such as PTFE (Teflon). This finding prompted us to study conditions that promote assembly of SC3 into amyloid-fibrils. Here, it is shown that SC3 adopts the amyloid state at the water-PTFE interface at high concentration (300 mug ml(-1)) and prolonged incubation (16 h). Moreover, it is shown that amyloid formation at both the water-air and water-PTFE interface is promoted by the cell wall components schizophyllan (beta-(1-3)beta-(1-6)-glucan) and beta-(1-3)-glucan. Hydrophobin concentration and cell wall polysaccharides thus contribute to the role of SC3 in formation of aerial hyphae and in hyphal attachment.