title: Multiparametric imaging of adhesive nanodomains at the surface of Candida albicans by atomic force microscopy.
abstract: Candida albicans is an opportunistic pathogen. It adheres to mammalian cells through a variety of adhesins that interact with host ligands. The spatial organization of these adhesins on the cellular interface is however poorly understood, mainly because of the lack of an instrument able to track single molecules on single cells. In this context, the atomic force microscope (AFM) makes it possible to analyze the force signature of single proteins on single cells. The present study is dedicated to the mapping of the adhesive properties of C. albicans cells. We observed that the adhesins at the cell surface were organized in nanodomains composed of free or aggregated mannoproteins. This was demonstrated by the use of functionalized AFM tips and synthetic amyloid forming/disrupting peptides. This direct visualization of amyloids nanodomains will help in understanding the virulence factors of C. albicans.
authors.affiliation: CNRS, LAAS, F-31400 Toulouse, France; Université de Toulouse, LAAS, F-31400 Toulouse, France; CNRS, UMR 7565, SRSMC, Vandœuvre-lès-Nancy, France; Université de Lorraine, UMR 7565, Faculté de Pharmacie, Nancy, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Formosa
authors.affiliation: CNRS, LAAS, F-31400 Toulouse, France; Université de Toulouse, LAAS, F-31400 Toulouse, France.
authors.forename: Marion
authors.initials: M
authors.lastname: Schiavone
authors.affiliation: INRA, UMR1319 Micalis, F-78352 Jouy-en-Josas, France; AgroParisTech, UMR Micalis, F-78850 Thiverval Grignon, France.
authors.forename: Anita
authors.initials: A
authors.lastname: Boisrame
authors.affiliation: INRA, UMR1319 Micalis, F-78352 Jouy-en-Josas, France; AgroParisTech, UMR Micalis, F-78850 Thiverval Grignon, France.
authors.forename: Mathias L
authors.initials: ML
authors.lastname: Richard
authors.affiliation: CNRS, UMR 7565, SRSMC, Vandœuvre-lès-Nancy, France; Université de Lorraine, UMR 7565, Faculté de Pharmacie, Nancy, France; ABC Platform®, Nancy, France.
authors.forename: Raphaël E
authors.initials: RE
authors.lastname: Duval
authors.affiliation: CNRS, LAAS, F-31400 Toulouse, France; Université de Toulouse, LAAS, F-31400 Toulouse, France. Electronic address: edague@laas.fr.
authors.forename: Etienne
authors.initials: E
authors.lastname: Dague
mesh_terms: D000682:Amyloid / Q000737:chemistry; D018441:Biofilms; D002176:Candida albicans / Q000378:metabolism*; D002448:Cell Adhesion; D002462:Cell Membrane / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D003208:Concanavalin A / Q000737:chemistry; D004129:Dimethylpolysiloxanes / Q000737:chemistry; D005353:Fibronectins / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008024:Ligands; D018625:Microscopy, Atomic Force / Q000379:methods*; D053758:Nanoparticles / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013696:Temperature
chemical_list: D000682:Amyloid; D004129:Dimethylpolysiloxanes; D005353:Fibronectins; D008024:Ligands; D010455:Peptides; D003208:Concanavalin A; C013830:baysilon
keywords: Adhesins; Atomic force microscopy; Candida albicans; Multiparametric AFM; Nanodomains