Rbt1 Protein Domains Analysis in Candida albicans Brings Insights into Hyphal Surface Modifications and Rbt1 Potential Role during Adhesion and Biofilm Formation
2013
Monniot , Céline (INRA , Jouy-En-Josas (France). UMR 1319 MICrobiologie de l'ALImentation au Service de la Santé Humaine) | Baudevin , Anita (INRA , Jouy-En-Josas (France). UMR 1319 MICrobiologie de l'ALImentation au Service de la Santé Humaine) | Da Costa , Gregory (INRA , Jouy-En-Josas (France). UMR 1319 MICrobiologie de l'ALImentation au Service de la Santé Humaine) | Chauvel , Murielle (Institut National de la Recherche AgronomiqueInstitut Pasteur de Paris, ParisParis(France). USC2019) | Sautour , Marc (INRA , Dijon (France). UMR 1347 Agroécologie) | Bougnoux , Marie-Elisabeth (Institut Pasteur de ParisInstitut National de la Recherche AgronomiqueUniversité Paris Descartes (Paris 5)Assistance Publique - Hôpitaux de Paris, ParisParisParisParis(France). Unité Biologie et Pathogénicité Fongiques, Département Génomes et GénétiqueUSC2019Sorbonne Paris CitéUnité de Parasitologie-Mycologie, Service de Microbiologie, Hôpital Necker-Enfants-Malades) | Bellon-Fontaine , Marie Noelle (INRA , Jouy-En-Josas (France). UMR 1319 MICrobiologie de l'ALImentation au Service de la Santé Humaine) | DALLE , FREDERIC (INRA , Dijon (France). UMR 1347 Agroécologie) | d'Enfert , Christophe (Institut Pasteur de ParisInstitut National de la Recherche Agronomique, ParisParis(France). Unité Biologie et Pathogénicité Fongiques, Département Génomes et GénétiqueUSC2019) | Richard , Mathias(auteur de correspondance) (INRA , Jouy-En-Josas (France). UMR 1319 MICrobiologie de l'ALImentation au Service de la Santé Humaine)
Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces independently of its morphological state, heterologous expression and promoter swap strategies were applied. The N-terminal domain with features typical of the Flo11 superfamily was found to be essential for adhesiveness to polystyrene through an increase in cell surface hydrophobicity. A 42 amino acid-long domain localized in the central part of the protein was shown to enhance the aggregation function. We demonstrated that a VTTGVVVVT motif within the 42 amino acid domain displayed a high beta-aggregation potential and was responsible for cell-to-cell interactions by promoting the aggregation of hyphae. Finally, we showed through constitutive expression that while Rbt1 was directly accessible to antibodies in hyphae, it was not so in yeast. Similar results were obtained for another cell wall protein, namely Iff8, and suggested that modification of the cell wall structure between yeast and hyphae can regulate the extracellular accessibility of cell wall proteins independently of gene regulation.
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تم تزويد هذا السجل من قبل Institut national de la recherche agronomique
