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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Public Library of Science (PLoS)
2013-01-01
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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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language | English |
last_indexed | 2024-12-22T16:53:44Z |
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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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