β-1,2-Mannosyltransferases 1 and 3 Participate ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
β-1,2-Mannosyltransferases 1 and 3 Participate in Yeast and Hyphae O- and N-Linked Mannosylation and Alter Candida albicans Fitness During Infection.
Auteur(s) :
Courjol, Flavie [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Jouault, Thierry [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Mille, Celine [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Hall, Rebecca [Auteur]
University of Aberdeen
Maes, Emmanuel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Sendid, Boualem [Auteur]
Lille Inflammation Research International Center (LIRIC) - U995
Lille Inflammation Research International Center - U 995 [LIRIC]
Mallet, Jean-Maurice [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gow Neil, A R [Auteur]
University of Aberdeen
Poulain, Daniel [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Fradin, Chantal [Auteur]
Lille Inflammation Research International Center (LIRIC) - U995
Lille Inflammation Research International Center - U 995 [LIRIC]
Lille Inflammation Research International Center - U 995 [LIRIC]
Jouault, Thierry [Auteur]

Lille Inflammation Research International Center - U 995 [LIRIC]
Mille, Celine [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Hall, Rebecca [Auteur]
University of Aberdeen
Maes, Emmanuel [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Sendid, Boualem [Auteur]

Lille Inflammation Research International Center (LIRIC) - U995
Lille Inflammation Research International Center - U 995 [LIRIC]
Mallet, Jean-Maurice [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Guerardel, Yann [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gow Neil, A R [Auteur]
University of Aberdeen
Poulain, Daniel [Auteur]

Lille Inflammation Research International Center - U 995 [LIRIC]
Fradin, Chantal [Auteur]

Lille Inflammation Research International Center (LIRIC) - U995
Lille Inflammation Research International Center - U 995 [LIRIC]
Titre de la revue :
Open forum infectious diseases
Nom court de la revue :
Open Forum Infect. Dis.
Numéro :
2
Pagination :
ofv116
Date de publication :
2015-09-01
Mot(s)-clé(s) en anglais :
beta-1,2-oligomannosides
fungal virulence
mannosyltransferase
O-mannosylation
Candida albicans
fungal virulence
mannosyltransferase
O-mannosylation
Candida albicans
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
β-1,2-mannosylation of Candida albicans glycoconjugates has been investigated through the identification of enzymes involved in the addition of β-1,2-oligomannosides (β-Mans) to phosphopeptidomannan and phospholipomannan. ...
Lire la suite >β-1,2-mannosylation of Candida albicans glycoconjugates has been investigated through the identification of enzymes involved in the addition of β-1,2-oligomannosides (β-Mans) to phosphopeptidomannan and phospholipomannan. β-1,2-oligomannosides are supposed to have virulence properties that they confer to these glycoconjugates. In a previous study, we showed that cell wall mannoproteins (CWMPs) harbor β-Mans in their O-mannosides; therefore, we analyzed their biosynthesis and impact on virulence. In this study, we demonstrate that O-mannans are heterogeneous and that α-mannosylated O-mannosides, which are biosynthesized by Mnt1 and Mnt2 α-1,2-mannosyltransferases, can be modified with β-Mans but only at the nonreducing end of α-1,2-mannotriose. β-1,2-mannosylation of this O-mannotriose depends on growth conditions, and it involves 2 β-1,2-mannosyltransferases, Bmt1 and Bmt3. These Bmts are essential for β-1,2-mannosylation of CWMPs and expression of β-Mans on germ tubes. A bmt1Δ mutant and a mutant expressing no β-Mans unexpectedly disseminated more in BALB/c mice, whereas they had neither attenuated nor enhanced virulence in C57BL/6 mice. In galectin (Gal)3 knockout mice, the reference strain was more virulent than in C57BL/6 mice, suggesting that the β-Mans innate receptor Gal3 is involved in C. albicans fitness during infection.Lire moins >
Lire la suite >β-1,2-mannosylation of Candida albicans glycoconjugates has been investigated through the identification of enzymes involved in the addition of β-1,2-oligomannosides (β-Mans) to phosphopeptidomannan and phospholipomannan. β-1,2-oligomannosides are supposed to have virulence properties that they confer to these glycoconjugates. In a previous study, we showed that cell wall mannoproteins (CWMPs) harbor β-Mans in their O-mannosides; therefore, we analyzed their biosynthesis and impact on virulence. In this study, we demonstrate that O-mannans are heterogeneous and that α-mannosylated O-mannosides, which are biosynthesized by Mnt1 and Mnt2 α-1,2-mannosyltransferases, can be modified with β-Mans but only at the nonreducing end of α-1,2-mannotriose. β-1,2-mannosylation of this O-mannotriose depends on growth conditions, and it involves 2 β-1,2-mannosyltransferases, Bmt1 and Bmt3. These Bmts are essential for β-1,2-mannosylation of CWMPs and expression of β-Mans on germ tubes. A bmt1Δ mutant and a mutant expressing no β-Mans unexpectedly disseminated more in BALB/c mice, whereas they had neither attenuated nor enhanced virulence in C57BL/6 mice. In galectin (Gal)3 knockout mice, the reference strain was more virulent than in C57BL/6 mice, suggesting that the β-Mans innate receptor Gal3 is involved in C. albicans fitness during infection.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Projet Européen :
Établissement(s) :
Inserm
Université de Lille
CHU Lille
CNRS
Université de Lille
CHU Lille
CNRS
Collections :
Équipe(s) de recherche :
Fungal associated invasive and inflammatory diseases
Nutritional modulation of inflammation and infection
IBD and environnemental factors : epidemiology and functional analyses
Nutritional modulation of inflammation and infection
IBD and environnemental factors : epidemiology and functional analyses
Date de dépôt :
2019-03-01T14:35:02Z
2021-03-25T08:00:41Z
2021-03-25T08:00:41Z
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