This entry represents class I hydrophobins found in fungi.

Hydrophobins are small, moderately hydrophobic extracellular proteins characterised by eight cysteine residues arranged in a strictly conserved motif. They are typically found on the outer surface of conidia and the hyphal wall, where they are thought to mediate contact and communication between the fungus and its environment … expand

This entry represents class I hydrophobins found in fungi.

Hydrophobins are small, moderately hydrophobic extracellular proteins characterised by eight cysteine residues arranged in a strictly conserved motif. They are typically found on the outer surface of conidia and the hyphal wall, where they are thought to mediate contact and communication between the fungus and its environment [ PUBMED:11343402 ]. The hydrophobin family includes proteins such as cryparin, a cell surface-associated hydrophobin secreted by filamentous fungi [ PUBMED:10584000 ]; cerato-ulmin, a secreted toxin implicated in Dutch elm disease [ PUBMED:9344630 ]; and trihydrophobin from Claviceps fusiformis, which self-assembles at hydrophilic-hydrophobic interfaces on the hyphal surface [ PUBMED:10336622 ]. Hydrophobins are broadly categorised into two classes based on their solubility and assembly properties. Class I hydrophobins form rodlet bundles that coat aerial cell surfaces and contribute to cellular hydrophobicity, supporting fungal growth, development, and dispersal. In contrast, Class II hydrophobins form highly ordered films at water-air interfaces via intermolecular interactions but do not form rodlet structures. Hyd1 is a class II hydrophobin that not only fulfils structural roles but also functions as an elicitor of induced systemic resistance (ISR) in plants. During interaction with maize, Hyd1 binds the host target protein UBL and recruits additional UBL proteins in the roots, triggering defence responses such as cell death and activation of brassinosteroid, jasmonate (JA), and ethylene (ET) signalling pathways [ PUBMED:3080312 ].