Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.

Candida albicans produces a complex glycosphingolipid called phospholipomannan (PLM), which is present on the cell-wall surface of yeast and shed upon contact with host cells. The glycan moiety of PLM is composed of β-mannosides with degrees of polymerization up to 19 in C. albicans serotype A. PLM...

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Main Authors: Audrey Devillers, Flavie Courjol, Chantal Fradin, Agnes Coste, Daniel Poulain, Bernard Pipy, Emerson Soares Bernardes, Thierry Jouault
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3868656?pdf=render
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author Audrey Devillers
Flavie Courjol
Chantal Fradin
Agnes Coste
Daniel Poulain
Bernard Pipy
Emerson Soares Bernardes
Thierry Jouault
author_facet Audrey Devillers
Flavie Courjol
Chantal Fradin
Agnes Coste
Daniel Poulain
Bernard Pipy
Emerson Soares Bernardes
Thierry Jouault
author_sort Audrey Devillers
collection DOAJ
description Candida albicans produces a complex glycosphingolipid called phospholipomannan (PLM), which is present on the cell-wall surface of yeast and shed upon contact with host cells. The glycan moiety of PLM is composed of β-mannosides with degrees of polymerization up to 19 in C. albicans serotype A. PLM from serotype B strains displays a twofold decrease in the length of the glycan chains. In this study we compared the proinflammatory activities of PLMs purified from C. albicans serotype A and serotype B strains and from a bmt6Δ mutant of C. albicans, whose PLM is composed of short truncated oligomannosidic chain. We found that PLMs activate caspase-1 in murine macrophage cell line J774 independent of the glycan chain length although IL-1β secretion is more intense with long glycan chain. None of the tested PLMs stimulate ROS production, indicating that caspase-1 activation may occur through a ROS-independent pathway. On the other hand, only long-chain oligomannosides present on PLM from serotype A strain (PLM-A) are able to induce TNF-α production in macrophages, a property that is not affect by blocking endocytosis through latrunculin A treatment. Finally, we demonstrate that soluble and not cell surface-bound galectin-3, is able to potentiate PLM-A-induced TNF-α production in macrophages. PLMs from C. albicans serotype B and from bmt6∆ mutant are not able to induce TNF-α production and galectin-3 pretreatment does not interfere with this result. In conclusion, we show here that PLMs are able to evoke a proinflammatory state in macrophage, which is in part dependent on their glycosylation status. Long-glycan chains favor interaction with soluble galectin-3 and help amplify inflammatory response.
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spelling doaj.art-c21a427b482f4c1cae8262ef264069f82022-12-21T18:19:31ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-01812e8477110.1371/journal.pone.0084771Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.Audrey DevillersFlavie CourjolChantal FradinAgnes CosteDaniel PoulainBernard PipyEmerson Soares BernardesThierry JouaultCandida albicans produces a complex glycosphingolipid called phospholipomannan (PLM), which is present on the cell-wall surface of yeast and shed upon contact with host cells. The glycan moiety of PLM is composed of β-mannosides with degrees of polymerization up to 19 in C. albicans serotype A. PLM from serotype B strains displays a twofold decrease in the length of the glycan chains. In this study we compared the proinflammatory activities of PLMs purified from C. albicans serotype A and serotype B strains and from a bmt6Δ mutant of C. albicans, whose PLM is composed of short truncated oligomannosidic chain. We found that PLMs activate caspase-1 in murine macrophage cell line J774 independent of the glycan chain length although IL-1β secretion is more intense with long glycan chain. None of the tested PLMs stimulate ROS production, indicating that caspase-1 activation may occur through a ROS-independent pathway. On the other hand, only long-chain oligomannosides present on PLM from serotype A strain (PLM-A) are able to induce TNF-α production in macrophages, a property that is not affect by blocking endocytosis through latrunculin A treatment. Finally, we demonstrate that soluble and not cell surface-bound galectin-3, is able to potentiate PLM-A-induced TNF-α production in macrophages. PLMs from C. albicans serotype B and from bmt6∆ mutant are not able to induce TNF-α production and galectin-3 pretreatment does not interfere with this result. In conclusion, we show here that PLMs are able to evoke a proinflammatory state in macrophage, which is in part dependent on their glycosylation status. Long-glycan chains favor interaction with soluble galectin-3 and help amplify inflammatory response.http://europepmc.org/articles/PMC3868656?pdf=render
spellingShingle Audrey Devillers
Flavie Courjol
Chantal Fradin
Agnes Coste
Daniel Poulain
Bernard Pipy
Emerson Soares Bernardes
Thierry Jouault
Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.
PLoS ONE
title Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.
title_full Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.
title_fullStr Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.
title_full_unstemmed Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.
title_short Deficient beta-mannosylation of Candida albicans phospholipomannan affects the proinflammatory response in macrophages.
title_sort deficient beta mannosylation of candida albicans phospholipomannan affects the proinflammatory response in macrophages
url http://europepmc.org/articles/PMC3868656?pdf=render
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