Title :

Candida albicans beta-1,2-mannosyltransferase Bmt3 prompts the elongation of the cell-wall phosphopeptidomannan

Author(s) :

Sfihi-Loualia, Ghenima [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Hurtaux, Thomas [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fabre, Emeline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fradin, Chantal [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Mee, Anais [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Pourcelot, Marilyne [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Maes, Emmanuel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Mallet, Jean-Maurice [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Poulain, Daniel [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Delplace, Florence [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]

Journal title :

Glycobiology

Abbreviated title :

Glycobiology

Volume number :

26

Pages :

203-214

Publication date :

2016-02-01

English keyword(s) :

mannosyltransferase
cell wall
Candida albicans
beta-mannose
yeast

HAL domain(s) :

Sciences du Vivant [q-bio]

English abstract : [en]

β-1,2-Linked mannosides are expressed on numerous cell-wall glycoconjugates of the opportunisticpathogen yeastCandida albicans. Several studies evidenced their implication in the host–pathogeninteraction and virulence ...
Show more >β-1,2-Linked mannosides are expressed on numerous cell-wall glycoconjugates of the opportunisticpathogen yeastCandida albicans. Several studies evidenced their implication in the host–pathogeninteraction and virulence mechanisms. In the present study, we characterized the in vitro activity ofCaBmt3, aβ-1,2-mannosyltransferase involved in the elongation ofβ-1,2-oligomannosides oligo-mers onto the cell-wall polymannosylatedN-glycans. A recombinant soluble enzyme Bmt3p wasproduced inPichia pastorisand its enzyme activity was investigated using natural and synthetic oli-gomannosides as potential acceptor substrates. Bmt3p was shown to exhibit an exquisite enzymaticspecificity by adding a single terminalβ-mannosyl residue toα-1,2-linked oligomannosides cappedby a Manβ1–2Man motif. Furthermore, we demonstrated that the previously identified CaBmt1 andCaBmt3 efficiently act together to generate Manβ1-2Manβ1–2[Manα1–2]nsequence fromα-1,2-linkedoligomannosides onto exogenous and endogenous substrates.Show less >

Language :

Anglais

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

Inserm
Université de Lille
CHU Lille
CNRS

Collections :

• Institut de Recherche Translationnelle sur l'Inflammation (INFINITE) - U1286
• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Fungal associated invasive and inflammatory diseases
IBD and environnemental factors : epidemiology and functional analyses

Submission date :

2019-03-01T15:15:46Z
2021-03-19T07:03:31Z
2021-03-19T07:15:37Z