News Column

New Findings in Aspergillus Described from University of Pau and Pays de l'Adour

June 27, 2014



By a News Reporter-Staff News Editor at Health & Medicine Week -- Researchers detail new data in Aspergillus. According to news reporting out of Pau, France, by NewsRx editors, research stated, "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."

Our news journalists obtained a quote from the research from the University of Pau and Pays de l'Adour, "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."

According to the news editors, the research concluded: "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."

For more information on this research see: 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):1137-1144. Biochimica Et Biophysica Acta-Proteins and Proteomics can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands (see also Aspergillus).

Our news journalists report that additional information may be obtained by contacting A. Zykwinska, Univ Pau & Pays Adour, CNRS, UMR 5254, IPREM Equips Phys & Chim Polymeres, F-64053 Pau, France. Additional authors for this research include M. Pihet, S. Radji, J.P. Bouchara and S. Cuenot.

Keywords for this news article include: Pau, France, Europe, Aspergillus Fumigatus

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Source: Health & Medicine Week