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

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• 作者：Ariane Pille (1) (2) (3)
  Ann H. Kwan (4)
  Ivan Cheung (4)
  Matthew Hampsey (4)
  Vishukumar Aimanianda (6)
  Muriel Delepierre (1) (2)
  Jean-Paul Latg茅 (6)
  Margaret Sunde (5)
  J. I帽aki Guijarro (1) (2)
  
  1. Unit茅 de RMN des Biomol茅cules ; D茅pt. Biologie Structurale et Chimie ; Institut Pasteur ; 25 rue Du Dr. Roux ; 75015 ; Paris ; France
  2. CNRS UMR 3528 ; 75015 ; Paris ; France
  3. Sorbonne Universit茅s ; UPMC Univ Paris 06 ; IFD ; 4 Place Jussieu ; 75252 ; Paris Cedex 05 ; France
  4. School of Molecular Bioscience ; University of Sydney ; Sydney ; NSW ; 2006 ; Australia
  6. Unit茅 des Aspergillus ; D茅pt de Parasitologie et Mycologie ; Institut Pasteur ; 28 rue Du Dr. Roux ; 75015 ; Paris ; France
  5. School of Medical Sciences ; University of Sydney ; Sydney ; NSW ; 2006 ; Australia
  
• 关键词：Hydrophobin ; Functional amyloids ; Rodlets ; Cell wall ; Aspergillus fumigatus ; NMR
• 刊名：Biomolecular NMR Assignments
• 出版年：2015
• 出版时间：April 2015
• 年：2015
• 卷：9
• 期：1
• 页码：113-118
• 全文大小：1,178 KB
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  12. Morris, VK, Ren, Q, Macindoe, I, Kwan, AH, Byrne, N, Sunde, M (2011) Recruitment of class I hydrophobins to the air:water interface initiates a multi-step process of functional amyloid formation. J Biol Chem 286: pp. 15955-15963 CrossRef
  13. Morris VK, Kwan AH, Mackay JP, Sunde M (2012) Backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments of the hydrophobin DewA from / Aspergillus nidulans. Biomol NMR Assign 6:83鈥?6
  14. Morris, VK, Kwan, AH, Sunde, M (2013) Analysis of the structure and conformational states of DewA gives insight into the assembly of the fungal hydrophobins. J Mol Biol 425: pp. 244-256 CrossRef
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• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

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 1H, 13C and 15N resonance assignments of the soluble monomeric form of RodA.