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Zykwinska, A., Pihet, M., Radji, S., Bouchara, J.-P. & Cuenot, S. (2014) Self-assembly of proteins into a three-dimensional multilayer system: Investigation of the surface of the human fungal pathogen Aspergillus fumigatus. BBA-Proteins Proteomics, 1844 1137–1144. 
Added by: Laurent Cournède (2016-03-10 21:01:56)
Type de référence: Article
DOI: 10.1016/j.bbapap.2014.03.001
Numéro d'identification (ISBN etc.): 1570-9639
Clé BibTeX: Zykwinska2014a
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Catégories: PMN
Mots-clés: amyloid-like fibrils, Anisotropic interaction, Aspergillus fumigatus, cell-wall, chemical-composition, conidia, dynamics, eas, encodes, hydrophobin sc3, Monte Carlo simulation, RodA hydrophobin, Rodlet, rodlet layer, Self-assembly, simulations
Créateurs: Bouchara, Cuenot, Pihet, Radji, Zykwinska
Collection: BBA-Proteins Proteomics
Consultations : 1/549
Indice de consultation : 4%
Indice de popularité : 1%
Résumé     
Hydrophobins are small surface active proteins that fulfil a wide spectrum of functions in fungal growth and development. The human fungal pathogen Aspergillus fumigatus expresses RodA hydrophobins that self-assemble on the outer conidial surface into tightly organized nanorods known as rodlets. AFM investigation of the conidial surface allows us to evidence that RodA hydrophobins self-assemble into rodlets through bilayers. Within bilayers, hydrophilic domains of hydrophobins point inward, thus making a hydrophilic core, while hydrophobic domains point outward. AFM measurements reveal that several rodlet bilayers are present on the conidial surface thus showing that proteins self-assemble into a complex three-dimensional multilayer system. The self-assembly of RodA hydrophobins into rodlets results from attractive interactions between stacked beta-sheets, which conduct to a final linear cross-beta spine structure. A Monte Carlo simulation shows that anisotropic interactions are the main driving forces leading the hydrophobins to self-assemble into parallel rodlets, which are further structured in nanodomains. Taken together, these findings allow us to propose a mechanism, which conducts RodA hydrophobins to a highly ordered rodlet structure. The mechanism of hydrophobin assembly into rodlets offers new prospects for the development of more efficient strategies leading to disruption of rodlet formation allowing a rapid detection of the fungus by the immune system. (C) 2014 Elsevier B.V. All rights reserved.
Added by: Laurent Cournède  
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