Publication:
Glycoconjugate expression on the cell wall of tps1/tps1 trehalose-deficient Candida albicans strain and implications for its interaction with macrophages

dc.contributor.authorVitse-Standaert, Annie
dc.contributor.authorGarcía-Peñarrubia, Pilar
dc.contributor.authorArgüelles, Juan Carlos
dc.contributor.authorPoulain, Daniel
dc.contributor.authorJouault, Thierry
dc.contributor.authorMartínez-Esparza Alvargonzález, María Concepción
dc.contributor.authorTapia Abellán, Ana
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-07-02T08:34:04Z
dc.date.available2024-07-02T08:34:04Z
dc.date.issued2011-01-20
dc.description© The Author 2011. This document is the Published version of a Published Work that appeared in final form in Glycobiology. To access the final edited and published work see https://doi.org/10.1093/glycob/cwr007
dc.description.abstractThe yeast Candida albicans has developed a variety of strategies to resist macrophage killing. In yeasts, accumulation of trehalose is one of the principal defense mechanisms under stress conditions. The gene-encoding trehalose-6-phosphate synthase (TPS1), which is responsible for trehalose synthesis, is induced in response to oxidative stress, as in phagolysosomes. Mutants unable to synthesize trehalose are sensitive to oxidative stress in vitro. In mice, the TPS1-deficient strain, tps1/tps1, displays a lower infection rate than its parental strain (CAI4). We have previously demonstrated the reduced binding capacity of tps1/tps1 and its lower resistance to macrophages. At the same time, its outer cell wall layer was seen to be altered. In this study, we show that depending on the culture conditions, the tps1/tps1 strain regulates the carbohydrate metabolism in a different way to CAI4, as reflected by the enhanced β-mannosylation of cell wall components, especially at the level of the 120 kDa glycoprotein species, accessible at the cell surface of tps1/tps1 when cultured in liquid medium, but not on solid medium. This leads to changes in its surface properties, as revealed by decreased hydrophobicity, and the lower levels of ERK1/2 phosphorylation and tumor necrosis factor-α (TNF-α) production in macrophages, thus increasing the resistance to these cells. In contrast, in solid medium, in which over-glycosylation was less evident, tps1/tps1 showed similar macrophage interaction properties to CAI4, but was less resistant to killing, confirming the protective role of trehalose. Thus, the lack of trehalose is compensated by an over-glycosylation of the cell wall components in the tps1/tps1 mutant, which reduces susceptibility to killing.es
dc.formatapplication/pdfes
dc.format.extent10es
dc.identifier.citationGlycobiology 21(6):796-805, 2011
dc.identifier.doihttps://doi.org/10.1093/glycob/cwr007
dc.identifier.issnPrint: 0959-6658
dc.identifier.issnElectronic: 1460-2423
dc.identifier.urihttp://hdl.handle.net/10201/142799
dc.languageenges
dc.publisherOxford University Presses
dc.relationThis work was supported in part by the project BIO-BMC 06/01-0003 from DGI, Comunidad de Murcia, Spain. MM-E and AT-A were supported by the Fundación Séneca, Comunidad de Murcia, Spain.es
dc.relation.publisherversionhttps://academic.oup.com/glycob/article/21/6/796/1991071?login=truees
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectCandida albicanses
dc.subjectCell walles
dc.subjectMacrophageses
dc.subjectTrehalosees
dc.titleGlycoconjugate expression on the cell wall of tps1/tps1 trehalose-deficient Candida albicans strain and implications for its interaction with macrophageses
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
relation.isAuthorOfPublication79449fb4-f715-4255-a064-bfecc4b502de
relation.isAuthorOfPublication0ef289d2-ad85-4d81-a66c-82879daf26a9
relation.isAuthorOfPublication.latestForDiscovery79449fb4-f715-4255-a064-bfecc4b502de
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