1H, 13C and 15N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus

Ariane Pille,Vishukumar Aimanianda,Muriel Delepierre,Ivan Cheung,Ann H Kwan,J Iñaki Guijarro,Matthew Hampsey,Margaret Sunde,Jean-Paul Latgé

doi:10.1007/s12104-014-9555-1

Abstract

Hydrophobins are fungal proteins characterised by their amphipathic properties and an idiosyncratic pattern of eight cysteine residues involved in four disulphide bridges. The soluble form of these proteins spontaneously self-assembles at hydrophobic/hydrophilic interfaces to form an amphipathic monolayer. The RodA hydrophobin of the opportunistic pathogen Aspergillus fumigatus forms an amyloid layer with a rodlet morphology that covers the surface of fungal spores. This rodlet layer bestows hydrophobicity to the spores facilitating their dispersal in the air and rendering the conidia inert relative to the human immune system. As a first step in the analysis of the solution structure and self-association of RodA, we report the (1)H, (13)C and (15)N resonance assignments of the soluble monomeric form of RodA.

Highlights

Hydrophobins are small (< 20 kDa) amphipathic proteins produced by most filamentous fungi
These proteins with remarkable physicochemical properties are defined by a pattern of eight cysteine (Cys) residues that form four disulphide bonds (C1−C6, C2−C5, C3−C4, C7−C8) (Kwan et al 2006). They are produced in a soluble form that spontaneously self-assembles at hydrophobic/hydrophilic or air/water interfaces to form amphipathic monolayers with high surfactant activity
The structures of the soluble forms of hydrophobins from both classes that self-associate into monolayers are quite different but show a common central β-barrel stabilised by the four disulphide bridges and surrounding loops of different length and secondary structure (Sunde et al 2008)

Summary

Introduction

Hydrophobins are small (< 20 kDa) amphipathic proteins produced by most filamentous fungi. The structures of the soluble forms of hydrophobins from both classes that self-associate into monolayers are quite different but show a common central β-barrel stabilised by the four disulphide bridges and surrounding loops of different length and secondary structure (Sunde et al 2008).

Results

Conclusion