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Article Dans Une Revue Biochimica et Biophysica Acta Proteins and Proteomics Année : 2014

Self-assembly of proteins into a three-dimensional multilayer system: Investigation of the surface of the human fungal pathogen Aspergillus fumigatus

A. Zykwinska
  • Fonction : Auteur
M. Pihet
  • Fonction : Auteur
J.-P. Bouchara
  • Fonction : Auteur

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 β-sheets, which conduct to a final linear cross-β 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. © 2014 Elsevier B.V.

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Dates et versions

hal-01615977 , version 1 (12-10-2017)

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A. Zykwinska, M. Pihet, Sadia Radji, J.-P. Bouchara, S. Cuenot. Self-assembly of proteins into a three-dimensional multilayer system: Investigation of the surface of the human fungal pathogen Aspergillus fumigatus. Biochimica et Biophysica Acta Proteins and Proteomics, 2014, 1844 (6), pp.1137-1144. ⟨10.1016/j.bbapap.2014.03.001⟩. ⟨hal-01615977⟩
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