N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence

Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for correct protein localization, secretion and f...

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Autores: Marín Menguiano, Miriam, Moreno-Sánchez, Ismael, Ramos Barrales, Ramón, Fernandez Alvarez, Alfonso, Ibeas, José
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad Pablo de Olavide (UPO)
Repositorio:RIO. Repositorio Institucional Olavide
Idioma:inglés
OAI Identifier:oai:rio.upo.es:10433/26114
Acceso en línea:https://hdl.handle.net/10433/26114
Access Level:acceso abierto
Palabra clave:Ustilago maydis
Smut fungi
Pathogenesis
Pdi
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spelling N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulenceMarín Menguiano, MiriamMoreno-Sánchez, IsmaelRamos Barrales, RamónFernandez Alvarez, AlfonsoIbeas, JoséUstilago maydisSmut fungiPathogenesisPdiFungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for correct protein localization, secretion and function. Thus, the absence of glycosylation is associated with animal and plant pathogen avirulence. While the relevance of protein glycosylation for pathogenesis has been well established, the main glycoproteins responsible for the loss of virulence observed in glycosylation-defective fungi have not been identified. Here, we devise a proteomics approach to identify such proteins and use it to demonstrate a role for the highly conserved protein disulfide isomerase Pdi1 in virulence. We show that efficient Pdi1 N-glycosylation, which promotes folding into the correct protein conformation, is required for full pathogenic development of the corn smut fungus Ustilago maydis. Remarkably, the observed virulence defects are reminiscent of those seen in glycosylation-defective cells suggesting that the N-glycosylation of Pdi1 is necessary for the full secretion of virulence factors. All these observations, together with the fact that Pdi1 protein and RNA expression levels rise upon virulence program induction, suggest that Pdi1 glycosylation is important for normal pathogenic development in U. maydis. Our results provide new insights into the role of glycosylation in fungal pathogenesis.PLOS20262026-02-1720192019-11-1520192019-11-15journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10433/26114reponame:RIO. Repositorio Institucional Olavideinstname:Universidad Pablo de Olavide (UPO)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:rio.upo.es:10433/261142026-06-13T12:46:27Z
dc.title.none.fl_str_mv N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
title N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
spellingShingle N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
Marín Menguiano, Miriam
Ustilago maydis
Smut fungi
Pathogenesis
Pdi
title_short N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
title_full N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
title_fullStr N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
title_full_unstemmed N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
title_sort N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
dc.creator.none.fl_str_mv Marín Menguiano, Miriam
Moreno-Sánchez, Ismael
Ramos Barrales, Ramón
Fernandez Alvarez, Alfonso
Ibeas, José
author Marín Menguiano, Miriam
author_facet Marín Menguiano, Miriam
Moreno-Sánchez, Ismael
Ramos Barrales, Ramón
Fernandez Alvarez, Alfonso
Ibeas, José
author_role author
author2 Moreno-Sánchez, Ismael
Ramos Barrales, Ramón
Fernandez Alvarez, Alfonso
Ibeas, José
author2_role author
author
author
author
dc.contributor.none.fl_str_mv
dc.subject.none.fl_str_mv Ustilago maydis
Smut fungi
Pathogenesis
Pdi
topic Ustilago maydis
Smut fungi
Pathogenesis
Pdi
description Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for correct protein localization, secretion and function. Thus, the absence of glycosylation is associated with animal and plant pathogen avirulence. While the relevance of protein glycosylation for pathogenesis has been well established, the main glycoproteins responsible for the loss of virulence observed in glycosylation-defective fungi have not been identified. Here, we devise a proteomics approach to identify such proteins and use it to demonstrate a role for the highly conserved protein disulfide isomerase Pdi1 in virulence. We show that efficient Pdi1 N-glycosylation, which promotes folding into the correct protein conformation, is required for full pathogenic development of the corn smut fungus Ustilago maydis. Remarkably, the observed virulence defects are reminiscent of those seen in glycosylation-defective cells suggesting that the N-glycosylation of Pdi1 is necessary for the full secretion of virulence factors. All these observations, together with the fact that Pdi1 protein and RNA expression levels rise upon virulence program induction, suggest that Pdi1 glycosylation is important for normal pathogenic development in U. maydis. Our results provide new insights into the role of glycosylation in fungal pathogenesis.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-11-15
2019
2019-11-15
2026
2026-02-17
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/10433/26114
url https://hdl.handle.net/10433/26114
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv PLOS
publisher.none.fl_str_mv PLOS
dc.source.none.fl_str_mv reponame:RIO. Repositorio Institucional Olavide
instname:Universidad Pablo de Olavide (UPO)
instname_str Universidad Pablo de Olavide (UPO)
reponame_str RIO. Repositorio Institucional Olavide
collection RIO. Repositorio Institucional Olavide
repository.name.fl_str_mv
repository.mail.fl_str_mv
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