Fungal Fibrils: Application of the Amyloid Polymer Structure by Fungi - The Functional Fold: Amyloid Structures in Nature - page 35

Chapter 3

Fungal Fibrils: Application of the
Amyloid Polymer Structure by Fungi

Margaret Sunde, a Matthew D. Templeton, b and Ann H. Kwan a
a

School of Molecular Bioscience, University of Sydney,
Sydney 2006, Australia
b

The Horticultural and Food Research Institute of New Zealand,
Mt Albert Research Centre, Auckland, New Zealand
[e-mail]

Hydrophobins are low molecular weight proteins found ubiquitously
in filamentous fungi. They are secreted as soluble monomers, but
polymerize spontaneously at hydrophobic/hydrophilic interfaces
to coat aerial structures such as conidia and fruiting bodies.
Hydrophobins play multiple roles in fungal biology, ranging from
conferring water resistance to fungal structures, to assisting the
formation of aerial hyphae by reducing the surface tension of
the growth medium, as well as mediating interactions between
the fungus and its environment or host. Many hydrophobins
polymerize into fibrillar assemblies (known as rodlets) that closely
resemble amyloid fibrils, both in terms of structure and physical
properties. In addition, the rodlets assemble laterally into monolayers
that are amphipathic. Hydrophobin rodlets therefore represent an
application of the amyloid structural scaffold by nature to serve