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https://doi.org/10.1093/femsyr/foy124
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Cabello, Laura | - |
dc.contributor.author | Gómez Herreros, Estefanía | - |
dc.contributor.author | Fernández Pereira, Jordan | - |
dc.contributor.author | Maicas, Sergi | - |
dc.contributor.author | Martínez Esparza, M. | - |
dc.contributor.author | Groot, Piet W. J. de | - |
dc.contributor.author | Valentín, Eulogio | - |
dc.contributor.other | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular B e Inmunología | es |
dc.date.accessioned | 2024-06-26T11:45:11Z | - |
dc.date.available | 2024-06-26T11:45:11Z | - |
dc.date.issued | 2018-11-21 | - |
dc.identifier.citation | FEMS Yeast Research. 2019, Vol.. 19, N. 2, foy124 | es |
dc.identifier.issn | Print: 1567-1356 | - |
dc.identifier.issn | Electronic: 1567-1364 | - |
dc.identifier.uri | http://hdl.handle.net/10201/142688 | - |
dc.description | © FEMS 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ This document is the Published version of a Published Work that appeared in final form in FEMS Yeast Research. To access the final edited and published work see https://doi.org/10.1093/femsyr/foy124 | - |
dc.description.abstract | Candida albicans is a predominant cause of fungal infections in mucosal tissues as well as life-threatening bloodstream infections in immunocompromised patients. Within the human body, C. albicans is mostly embedded in biofilms, which provides increased resistance to antifungal drugs. The glyoxalase Glx3 is an abundant proteomic component of the biofilm extracellular matrix. Here, we document phenotypic studies of a glx3 null mutant concerning its role in biofilm formation, filamentation, antifungal drug resistance, cell wall integrity and virulence. First, consistent with its function as glyoxalase, the glx3 null mutant showed impaired growth on media containing glycerol as the carbon source and in the presence of low concentrations of hydrogen peroxide. Importantly, the glx3 mutant showed decreased fitness at 37◦C and formed less biofilm as compared to wild type and a reintegrant strain. At the permissive temperature of 28◦C, the glx3 mutant showed impaired filamentation as well as increased sensitivity to Calcofluor white, Congo red, sodium dodecyl sulfate and zymolyase, indicating subtle alterations in wall architecture even though gross quantitative compositional changes were not detected. Interestingly, and consistent with its impaired filamentation, biofilm formation and growth at 37◦C, the glx3 mutant is avirulent. Our results underline the role of Glx3 in fungal pathogenesis and the involvement of the fungal wall in this process. | es |
dc.format | application/pdf | es |
dc.format.extent | 7 | es |
dc.language | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation | This work was supported by two grants from MINECO (grant numbers PI12/01797, SAF2017-86188-P), both integrated in the Fondo Europeo de Desarrollo Regional (FEDER), and the first cofinanced by Instituto de Salud Carlos III (ISCIII). | es |
dc.rights | info:eu-repo/semantics/openAccess | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | C. albicans | es |
dc.subject | Candidiasis | es |
dc.subject | Glx3 protein | es |
dc.subject | Biofilms | es |
dc.subject | Cell wall | es |
dc.title | Deletion of GLX3 in Candida albicans affects temperature tolerance, biofilm formation, and virulence | es |
dc.type | info:eu-repo/semantics/article | es |
dc.relation.publisherversion | https://academic.oup.com/femsyr/article/19/2/foy124/5195521 | es |
dc.identifier.doi | https://doi.org/10.1093/femsyr/foy124 | - |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
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FEM Yest Res 2019.pdf | 3,04 MB | Adobe PDF | ![]() Visualizar/Abrir |
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