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

被引：0
作者：
Ariane Pille
Ann H. Kwan
Ivan Cheung
Matthew Hampsey
Vishukumar Aimanianda
Muriel Delepierre
Jean-Paul Latgé
Margaret Sunde
J. Iñaki Guijarro
机构：
[1] Unité de RMN des Biomolécules,School of Molecular Bioscience
[2] Dépt. Biologie Structurale et Chimie,School of Medical Sciences
[3] Institut Pasteur,undefined
[4] CNRS UMR 3528,undefined
[5] Sorbonne Universités,undefined
[6] University of Sydney,undefined
[7] University of Sydney,undefined
[8] Unité des Aspergillus,undefined
[9] Dépt de Parasitologie et Mycologie,undefined
[10] Institut Pasteur,undefined
来源：
Biomolecular NMR Assignments | 2015年 / 9卷
关键词：
Hydrophobin; Functional amyloids; Rodlets; Cell wall; NMR;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
引用
收藏
页码：113 / 118
页数：5
相关论文
共 128 条
[1]  
Aimanianda V(2009)Surface hydrophobin prevents immune recognition of airborne fungal spores Nature 460 1117-1121
[2]  
Bayry J(2012)Hydrophobins—unique fungal proteins PLoS Pathog 8 e1002700-14971
[3]  
Bozza S(2005)A simple method to predict protein flexibility using secondary chemical shifts J Am Chem Soc 127 14970-293
[4]  
Kniemeyer O(1995)NMRPipe: a multidimensional spectral processing system based on UNIX pipes J Biomol NMR 6 277-81
[5]  
Perruccio K(2005)Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements J Biomol NMR 32 71-367
[6]  
Elluru SR(2006)Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A Acta Crystallogr D Biol Crystallogr 62 356-2140
[7]  
Clavaud C(2006)Two crystal structures of Trichoderma reesei hydrophobin HFBI–the structure of a protein amphiphile with and without detergent interaction Protein Sci 15 2129-265
[8]  
Paris S(2013)Frequency, diagnosis and management of fungal respiratory infections Curr Opin Pulm Med 19 259-3626
[9]  
Brakhage AA(2006)Structural basis for rodlet assembly in fungal hydrophobins Proc Natl Acad Sci USA 103 3621-896
[10]  
Kaveri SV(2005)Hydrophobins: the protein-amphiphiles of filamentous fungi FEMS Microbiol Rev 29 877-811
12345678910