Hydrophobins are small, moderately hydrophobic proteins secreted by fu
ngi and containing eight cysteine residues in a conserved pattern. Mos
t hydrophobins have been discovered as putative products of genes abun
dantly expressed in development, pathogenesis and symbiosis. Those tha
t have been purified exhibit interfacial self-assembly into amphipathi
c protein films that can be extremely insoluble. These protein films a
rise at the surface of emergent structures, such as aerial hyphae, fru
it bodies and air-borne spores and they line air channels in tissues,
conferring hydrophobicity to these surfaces. Hydrophobins may also be
responsible for adherence of hyphae to each other and to hydrophobic s
urfaces of other organisms, as in pathogenic interactions.