title: Candida albicans β-1,2-mannosyltransferase Bmt3 prompts the elongation of the cell-wall phosphopeptidomannan.
abstract: β-1,2-Linked mannosides are expressed on numerous cell-wall glycoconjugates of the opportunistic pathogen yeast Candida albicans. Several studies evidenced their implication in the host-pathogen interaction and virulence mechanisms. In the present study, we characterized the in vitro activity of CaBmt3, a β-1,2-mannosyltransferase involved in the elongation of β-1,2-oligomannosides oligomers onto the cell-wall polymannosylated N-glycans. A recombinant soluble enzyme Bmt3p was produced in Pichia pastoris and its enzyme activity was investigated using natural and synthetic oligomannosides as potential acceptor substrates. Bmt3p was shown to exhibit an exquisite enzymatic specificity by adding a single terminal β-mannosyl residue to α-1,2-linked oligomannosides capped by a Manβ1-2Man motif. Furthermore, we demonstrated that the previously identified CaBmt1 and CaBmt3 efficiently act together to generate Manβ1-2Manβ1-2[Manα1-2]n sequence from α-1,2-linked oligomannosides onto exogenous and endogenous substrates.
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
authors.forename: Ghenima
authors.initials: G
authors.lastname: Sfihi-Loualia
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
authors.forename: Thomas
authors.initials: T
authors.lastname: Hurtaux
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
authors.forename: Emeline
authors.initials: E
authors.lastname: Fabre
authors.affiliation: Univ. Lille, Inserm, CHU Lille, U995 - LIRIC - Lille Inflammation Research International Center, F-59000 Lille, France.
authors.forename: Chantal
authors.initials: C
authors.lastname: Fradin
authors.affiliation: École Normale Supérieure-PSL Research University, Département de Chimie, Sorbonne Universités - UPMC Univ Paris 06, CNRS UMR 7203 LBM, 24, rue Lhomond, 75005 Paris, France.
authors.forename: Anaïs
authors.initials: A
authors.lastname: Mée
authors.affiliation: École Normale Supérieure-PSL Research University, Département de Chimie, Sorbonne Universités - UPMC Univ Paris 06, CNRS UMR 7203 LBM, 24, rue Lhomond, 75005 Paris, France.
authors.forename: Marilyne
authors.initials: M
authors.lastname: Pourcelot
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Maes
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
authors.forename: Julie
authors.initials: J
authors.lastname: Bouckaert
authors.affiliation: École Normale Supérieure-PSL Research University, Département de Chimie, Sorbonne Universités - UPMC Univ Paris 06, CNRS UMR 7203 LBM, 24, rue Lhomond, 75005 Paris, France.
authors.forename: Jean-Maurice
authors.initials: JM
authors.lastname: Mallet
authors.affiliation: Univ. Lille, Inserm, CHU Lille, U995 - LIRIC - Lille Inflammation Research International Center, F-59000 Lille, France.
authors.forename: Daniel
authors.initials: D
authors.lastname: Poulain
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France.
authors.forename: Florence
authors.initials: F
authors.lastname: Delplace
authors.affiliation: Univ. Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000 Lille, France yann.guerardel@univ-lille1.fr.
authors.forename: Yann
authors.initials: Y
authors.lastname: Guérardel
mesh_terms: D002175:Candida / Q000201:enzymology* / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D008351:Mannans / Q000378:metabolism*; D008364:Mannosyltransferases / Q000378:metabolism*; D010748:Phosphopeptides / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D005656:Fungal Proteins; D008351:Mannans; D010748:Phosphopeptides; C072108:phosphopeptidomannan; D008364:Mannosyltransferases
keywords: Candida albicans; cell wall; mannosyltransferase; yeast; β-mannose