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© Research
Publication : Biomolecular NMR assignments

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biomolecular NMR assignments - 01 Apr 2015

Pille A, Kwan AH, Cheung I, Hampsey M, Aimanianda V, Delepierre M, Latge JP, Sunde M, Guijarro JI

Link to Pubmed [PMID] – 24659460

Biomol NMR Assign 2015 Apr;9(1):113-8

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.

http://www.ncbi.nlm.nih.gov/pubmed/24659460