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In Candida parapsilosis the ATC1 gene encodes for an acid trehalase involved in trehalose hydrolysis, stress resistance and virulence

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dc.contributor.authorSánchez-Fresneda, Ruth
dc.contributor.authorMaicas, Sergi
dc.contributor.authorArgüelles, Juan-Carlos
dc.contributor.authorValentín, Eulogio
dc.contributor.authorMartínez-Esparza Alvargonzález, María Concepción
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2024-07-02T08:22:54Z
dc.date.available2024-07-02T08:22:54Z
dc.date.issued2014-06-12
dc.description© 2014 Sánchez-Fresneda et al. This manuscript version is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by/4.0/. This document is the Published version of a Published Work that appeared in final form in PLoS ONE. To access the final edited and published work see https://doi.org/10.1371/journal.pone.0099113
dc.description.abstractAn ORF named CPAR2-208980 on contig 005809 was identified by screening a Candida parapsilosis genome data base. Its 67% identity with the acid trehalase sequence from C. albicans (ATC1) led us to designate it CpATC1. Homozygous mutants that lack acid trehalase activity were constructed by gene disruption at the two CpATC1 chromosomal alleles. Phenotypic characterization showed that atc1Δ null cells were unable to grow on exogenous trehalose as carbon source, and also displayed higher resistance to environmental challenges, such as saline exposure (1.2 M NaCl), heat shock (42°C) and both mild and severe oxidative stress (5 and 50 mM H2O2). Significant amounts of intracellular trehalose were specifically stored in response to the thermal upshift in both wild type and mutant strains. Analysis of their antioxidant activities revealed that catalase was only triggered in response to heat shock in atc1Δ cells, whereas glutathione reductase was activated upon mild oxidative stress in wild type and reintegrant strains, and in response to the whole set of stress treatments in the homozygous mutant. Furthermore, yeast cells with double CpATC1 deletion were significantly attenuated in non-mammalian infection models, suggesting that CpATC1 is required for the pathobiology of the fungus. Our results demonstrate the involvement of CpAtc1 protein in the physiological hydrolysis of external trehalose in C. parapsilosis, where it also plays a major role in stress resistance and virulence.es
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dc.identifier.citationPLoS ONE 9(6): e99113
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0099113
dc.identifier.issnElectronic: 1932-6203
dc.identifier.urihttp://hdl.handle.net/10201/142797
dc.languageenges
dc.publisherPublic Library of Sciencees
dc.relationThe experimental work has been supported by grant PI12/01797 (Ministerio de Economı´a y Competitividad, ISCIII, Spain). The authors are also indebted to the financial contract provided by Cespa Servicios Urbanos de Murcia, S.A.es
dc.relation.publisherversionhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0099113es
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.titleIn Candida parapsilosis the ATC1 gene encodes for an acid trehalase involved in trehalose hydrolysis, stress resistance and virulencees
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
relation.isAuthorOfPublication79449fb4-f715-4255-a064-bfecc4b502de
relation.isAuthorOfPublication.latestForDiscovery79449fb4-f715-4255-a064-bfecc4b502de
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