Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum

Autores
Elhenawy, Wael; Scott, Nichollas E.; Tondo, Maria Laura; Orellano, Elena Graciela; Foster, Leonard J.; Feldman, Mario F.
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Ralstonia solanacearum is one of the most lethal phytopathogens in the world. Due to its broad host range, it can cause wilting disease in many plant species of economic interest. In this work, we identified the O-oligosaccharyltransferase (O-OTase) responsible for protein O-glycosylation in R. solanacearum. An analysis of the glycoproteome revealed that 20 proteins, including type IV pilins are substrates of this general glycosylation system. Although multiple glycan forms were identified, the majority of the glycopeptides were modified with a pentasaccharide composed of HexNAc-(Pen)-dHex3, similar to the O antigen subunit present in the lipopolysaccharide of multiple R. solanacearum strains. Disruption of the O-OTase led to the total loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. Comparative proteomic analysis revealed that the loss of glycosylation is not associated with widespread proteome changes. Only the levels of a single glycoprotein, the type IV pilin, were diminished in the absence of glycosylation. In parallel, disruption of glycosylation triggered an increase in the levels of a surface lectin homologous to Pseudomonas PA-IIL. These results reveal the important role of glycosylation in the pathogenesis of R. solanacearum.
Fil: Elhenawy, Wael. University of Alberta; Canadá
Fil: Scott, Nichollas E.. University of British Columbia; Canadá
Fil: Tondo, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Orellano, Elena Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Foster, Leonard J.. University of British Columbia; Canadá
Fil: Feldman, Mario F.. University of Alberta; Canadá. University of Washington; Estados Unidos
Materia
Biofilm
Protein O-Glycosylation
Type Iv Pili
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/52403
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearumElhenawy, WaelScott, Nichollas E.Tondo, Maria LauraOrellano, Elena GracielaFoster, Leonard J.Feldman, Mario F.BiofilmProtein O-GlycosylationType Iv Pilihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Ralstonia solanacearum is one of the most lethal phytopathogens in the world. Due to its broad host range, it can cause wilting disease in many plant species of economic interest. In this work, we identified the O-oligosaccharyltransferase (O-OTase) responsible for protein O-glycosylation in R. solanacearum. An analysis of the glycoproteome revealed that 20 proteins, including type IV pilins are substrates of this general glycosylation system. Although multiple glycan forms were identified, the majority of the glycopeptides were modified with a pentasaccharide composed of HexNAc-(Pen)-dHex3, similar to the O antigen subunit present in the lipopolysaccharide of multiple R. solanacearum strains. Disruption of the O-OTase led to the total loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. Comparative proteomic analysis revealed that the loss of glycosylation is not associated with widespread proteome changes. Only the levels of a single glycoprotein, the type IV pilin, were diminished in the absence of glycosylation. In parallel, disruption of glycosylation triggered an increase in the levels of a surface lectin homologous to Pseudomonas PA-IIL. These results reveal the important role of glycosylation in the pathogenesis of R. solanacearum.Fil: Elhenawy, Wael. University of Alberta; CanadáFil: Scott, Nichollas E.. University of British Columbia; CanadáFil: Tondo, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Orellano, Elena Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Foster, Leonard J.. University of British Columbia; CanadáFil: Feldman, Mario F.. University of Alberta; Canadá. University of Washington; Estados UnidosOxford University Press2015-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/52403Elhenawy, Wael; Scott, Nichollas E.; Tondo, Maria Laura; Orellano, Elena Graciela; Foster, Leonard J.; et al.; Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum; Oxford University Press; Glycobiology; 26; 3; 7-2015; 301-3110959-6658CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cwv098info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/glycob/article/26/3/301/2355395info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:15Zoai:ri.conicet.gov.ar:11336/52403instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:06:15.329CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
title Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
spellingShingle Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
Elhenawy, Wael
Biofilm
Protein O-Glycosylation
Type Iv Pili
title_short Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
title_full Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
title_fullStr Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
title_full_unstemmed Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
title_sort Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum
dc.creator.none.fl_str_mv Elhenawy, Wael
Scott, Nichollas E.
Tondo, Maria Laura
Orellano, Elena Graciela
Foster, Leonard J.
Feldman, Mario F.
author Elhenawy, Wael
author_facet Elhenawy, Wael
Scott, Nichollas E.
Tondo, Maria Laura
Orellano, Elena Graciela
Foster, Leonard J.
Feldman, Mario F.
author_role author
author2 Scott, Nichollas E.
Tondo, Maria Laura
Orellano, Elena Graciela
Foster, Leonard J.
Feldman, Mario F.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Biofilm
Protein O-Glycosylation
Type Iv Pili
topic Biofilm
Protein O-Glycosylation
Type Iv Pili
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Ralstonia solanacearum is one of the most lethal phytopathogens in the world. Due to its broad host range, it can cause wilting disease in many plant species of economic interest. In this work, we identified the O-oligosaccharyltransferase (O-OTase) responsible for protein O-glycosylation in R. solanacearum. An analysis of the glycoproteome revealed that 20 proteins, including type IV pilins are substrates of this general glycosylation system. Although multiple glycan forms were identified, the majority of the glycopeptides were modified with a pentasaccharide composed of HexNAc-(Pen)-dHex3, similar to the O antigen subunit present in the lipopolysaccharide of multiple R. solanacearum strains. Disruption of the O-OTase led to the total loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. Comparative proteomic analysis revealed that the loss of glycosylation is not associated with widespread proteome changes. Only the levels of a single glycoprotein, the type IV pilin, were diminished in the absence of glycosylation. In parallel, disruption of glycosylation triggered an increase in the levels of a surface lectin homologous to Pseudomonas PA-IIL. These results reveal the important role of glycosylation in the pathogenesis of R. solanacearum.
Fil: Elhenawy, Wael. University of Alberta; Canadá
Fil: Scott, Nichollas E.. University of British Columbia; Canadá
Fil: Tondo, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Orellano, Elena Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Foster, Leonard J.. University of British Columbia; Canadá
Fil: Feldman, Mario F.. University of Alberta; Canadá. University of Washington; Estados Unidos
description Ralstonia solanacearum is one of the most lethal phytopathogens in the world. Due to its broad host range, it can cause wilting disease in many plant species of economic interest. In this work, we identified the O-oligosaccharyltransferase (O-OTase) responsible for protein O-glycosylation in R. solanacearum. An analysis of the glycoproteome revealed that 20 proteins, including type IV pilins are substrates of this general glycosylation system. Although multiple glycan forms were identified, the majority of the glycopeptides were modified with a pentasaccharide composed of HexNAc-(Pen)-dHex3, similar to the O antigen subunit present in the lipopolysaccharide of multiple R. solanacearum strains. Disruption of the O-OTase led to the total loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. Comparative proteomic analysis revealed that the loss of glycosylation is not associated with widespread proteome changes. Only the levels of a single glycoprotein, the type IV pilin, were diminished in the absence of glycosylation. In parallel, disruption of glycosylation triggered an increase in the levels of a surface lectin homologous to Pseudomonas PA-IIL. These results reveal the important role of glycosylation in the pathogenesis of R. solanacearum.
publishDate 2015
dc.date.none.fl_str_mv 2015-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/52403
Elhenawy, Wael; Scott, Nichollas E.; Tondo, Maria Laura; Orellano, Elena Graciela; Foster, Leonard J.; et al.; Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum; Oxford University Press; Glycobiology; 26; 3; 7-2015; 301-311
0959-6658
CONICET Digital
CONICET
url http://hdl.handle.net/11336/52403
identifier_str_mv Elhenawy, Wael; Scott, Nichollas E.; Tondo, Maria Laura; Orellano, Elena Graciela; Foster, Leonard J.; et al.; Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum; Oxford University Press; Glycobiology; 26; 3; 7-2015; 301-311
0959-6658
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cwv098
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/glycob/article/26/3/301/2355395
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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