The Pga59 cell wall protein is an amyloid forming protein involved in adhesion and biofilm establishment in the pathogenic yeast Candida albicans
2023
Mourer, Thierry | El Ghalid, Mennat | Pehau-Arnaudet, Gérard | Kauffmann, Brice | Loquet, Antoine | Brûlé, Sébastien | Cabral, Vitor | D’enfert, Christophe | Bachellier-Bassi, Sophie | Biologie et Pathogénicité fongiques - Fungal Biology and Pathogenicity (BPF) ; Institut Pasteur [Paris] (IP)-Université Paris Cité (UPCité)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Plateforme BioImagerie Ultrastructurale – Ultrastructural BioImaging Platform (UTechS UBI) ; Institut Pasteur [Paris] (IP) | Biologie Moléculaire Structurale et Processus Infectieux (CNRS UMR3528) ; Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS) | Soutien à la Recherche de l'Institut Européen de Chimie Biologique ; Université Sciences et Technologies - Bordeaux 1 (UB)-Institut Européen de Chimie et de Biologie-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) | Chimie et Biologie des Membranes et des Nanoobjets (CBMN) ; Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS) | Biophysique Moléculaire (plateforme) - Molecular Biophysics (platform) ; Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité) | T.M. is a recipient of the Pasteur-Cantarini postdoctoral fellowship from the Institut Pasteur. M.E.G. was supported by Institut Pasteur Action Initiative Concertée Mycologie and V.C. was the recipient of a PhD fellowship from the European Commission (FINSysB, PITN-GA-2008-21400). The research work was conducted in the laboratory of C.dE. is supported by the French Government’s Investissement d’Avenir programme (Laboratoire d’Excellence Integrative Biology of Emerging Infectious Diseases, ANR-10-LABX-62-IBEID). This work has benefited from the Biophysical and Structural Chemistry Platform at IECB, CNRS UAR 3033, INSERM US001. We thank both UBI and PBI Core facilities from Institut Pasteur, and we are grateful for support for equipment from the French Government Programme Investissements d’Avenir France BioImaging (FBI, N° ANR-10-INSB-04-01). | ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010) | ANR-10-INBS-0004,France-BioImaging,Développment d'une infrastructure française distribuée coordonnée(2010) | European Project: 214004,PEOPLE,FP7-PEOPLE-2007-1-1-ITN,FINSYSB(2008)
International audience
Показать больше [+] Меньше [-]Английский. The human commensal fungus Candida albicans can attach to epithelia or indwelling medical devices and form biofilms, that are highly tolerant to antifungal drugs and can evade the immune response. The cell surface protein Pga59 has been shown to influence adhesion and biofilm formation. Here, we present evidence that Pga59 displays amyloid properties. Using electron microscopy, staining with an amyloid fibre-specific dye and X-ray diffraction experiments, we showed that the predicted amyloid-forming region of Pga59 is sufficient to build up an amyloid fibre in vitro and that recombinant Pga59 can also adopt a cross-β amyloid fibre architecture. Further, mutations impairing Pga59 amyloid assembly led to diminished adhesion to substrates and reduced biofilm production. Immunogold labelling on amyloid structures extracted from C. albicans revealed that Pga59 is used by the fungal cell to assemble amyloids within the cell wall in response to adhesion. Altogether, our results suggest that Pga59 amyloid properties are used by the fungal cell to mediate cell-substrate interactions and biofilm formation.
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