摘要
Understanding the molecular mechanism of the protein assembly still remains a challenge in the case of many biological systems. In this frame, the mechanism which drives RodA hydrophobins to self-assemble onto the surface of the conidia of the human fungal pathogen Aspergillus fumigatus into highly ordered nanorods known as rodlets, is still unresolved. Here, AFM investigations were combined with Monte Carlo simulations to elucidate how these small amphiphilic proteins self-assemble into tightly packed rodlets and how they are further organized in nanodomains. It becomes that the assembly of RodA hydrophobins into rodlets and their parallel alignment within nanodomains result from their anisotropic properties. Monte Carlo simulations allowed us to confirm that anisotropic interactions between macromolecules are sufficient to drive them to assembly into rodlets prior to nanodomains formation. Better knowledge of the mechanism of hydrophobins assembly into rodlets offers new prospects for the development of novel strategies leading to inhibition of rodlet formation, which should allow more rapid detection of the conidia by the immune system.
Understanding the molecular mechanism of the protein assembly still remains a challenge in the case of many biological systems. In this frame, the mechanism which drives RodA hydrophobins to self-assemble onto the surface of the conidia of the human fungal pathogen Aspergillus fumigatus into highly ordered nanorods known as rodlets, is still unresolved. Here, AFM investigations were combined with Monte Carlo simulations to elucidate how these small amphiphilic proteins self-assemble into tightly packed rodlets and how they are further organized in nanodomains. It becomes that the assembly of RodA hydrophobins into rodlets and their parallel alignment within nanodomains result from their anisotropic properties. Monte Carlo simulations allowed us to confirm that anisotropic interactions between macromolecules are sufficient to drive them to assembly into rodlets prior to nanodomains formation. Better knowledge of the mechanism of hydrophobins assembly into rodlets offers new prospects for the development of novel strategies leading to inhibition of rodlet formation, which should allow more rapid detection of the conidia by the immune system.
