title: (1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus.
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.
authors.forename: Ariane
authors.initials: A
authors.lastname: Pille
authors.forename: Ann H
authors.initials: AH
authors.lastname: Kwan
authors.forename: Ivan
authors.initials: I
authors.lastname: Cheung
authors.forename: Matthew
authors.initials: M
authors.lastname: Hampsey
authors.forename: Vishukumar
authors.initials: V
authors.lastname: Aimanianda
authors.forename: Muriel
authors.initials: M
authors.lastname: Delepierre
authors.forename: Jean-Paul
authors.initials: JP
authors.lastname: Latge
authors.forename: Margaret
authors.initials: M
authors.lastname: Sunde
authors.forename: J Iñaki
authors.initials: JI
authors.lastname: Guijarro
mesh_terms: D000595:Amino Acid Sequence; D001232:Aspergillus fumigatus; D005656:Fungal Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009894:Opportunistic Infections / Q000382:microbiology*; D017433:Protein Structure, Secondary
chemical_list: D005656:Fungal Proteins