Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells

Autores
Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; Pfrengle, Fabian; Bacic, Antony; Estevez, Jose Manuel
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.
Fil: Strasser, Richard. University of Natural Resources and Life Sciences; Suiza
Fil: Seifert, Georg. University of Natural Resources and Life Sciences; Suiza
Fil: Doblin, Monika S.. La Trobe University; Australia
Fil: Johnson, Kim L.. La Trobe University; Australia
Fil: Ruprecht, Colin. University of Natural Resources and Life Sciences; Suiza
Fil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; Suiza
Fil: Bacic, Antony. La Trobe University; Australia
Fil: Estevez, Jose Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Materia
ARABIDOPSIS
GLYCAN ARRAYS
GLYCAN FUNCTIONS
GLYCOSYL HYDROLASES
GLYCOSYLTRANSFERASES
N-GLYCOSYLATION
O-GLYCOSYLATION
PLANT PROTEIN GLYCOSYLATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/141685

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network_name_str CONICET Digital (CONICET)
spelling Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants CellsStrasser, RichardSeifert, GeorgDoblin, Monika S.Johnson, Kim L.Ruprecht, ColinPfrengle, FabianBacic, AntonyEstevez, Jose ManuelARABIDOPSISGLYCAN ARRAYSGLYCAN FUNCTIONSGLYCOSYL HYDROLASESGLYCOSYLTRANSFERASESN-GLYCOSYLATIONO-GLYCOSYLATIONPLANT PROTEIN GLYCOSYLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.Fil: Strasser, Richard. University of Natural Resources and Life Sciences; SuizaFil: Seifert, Georg. University of Natural Resources and Life Sciences; SuizaFil: Doblin, Monika S.. La Trobe University; AustraliaFil: Johnson, Kim L.. La Trobe University; AustraliaFil: Ruprecht, Colin. University of Natural Resources and Life Sciences; SuizaFil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; SuizaFil: Bacic, Antony. La Trobe University; AustraliaFil: Estevez, Jose Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFrontiers Media2021-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/141685Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-191664-462XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.640919/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2021.640919info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:59Zoai:ri.conicet.gov.ar:11336/141685instacron: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 10:04:59.445CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
title Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
spellingShingle Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
Strasser, Richard
ARABIDOPSIS
GLYCAN ARRAYS
GLYCAN FUNCTIONS
GLYCOSYL HYDROLASES
GLYCOSYLTRANSFERASES
N-GLYCOSYLATION
O-GLYCOSYLATION
PLANT PROTEIN GLYCOSYLATION
title_short Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
title_full Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
title_fullStr Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
title_full_unstemmed Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
title_sort Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
dc.creator.none.fl_str_mv Strasser, Richard
Seifert, Georg
Doblin, Monika S.
Johnson, Kim L.
Ruprecht, Colin
Pfrengle, Fabian
Bacic, Antony
Estevez, Jose Manuel
author Strasser, Richard
author_facet Strasser, Richard
Seifert, Georg
Doblin, Monika S.
Johnson, Kim L.
Ruprecht, Colin
Pfrengle, Fabian
Bacic, Antony
Estevez, Jose Manuel
author_role author
author2 Seifert, Georg
Doblin, Monika S.
Johnson, Kim L.
Ruprecht, Colin
Pfrengle, Fabian
Bacic, Antony
Estevez, Jose Manuel
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ARABIDOPSIS
GLYCAN ARRAYS
GLYCAN FUNCTIONS
GLYCOSYL HYDROLASES
GLYCOSYLTRANSFERASES
N-GLYCOSYLATION
O-GLYCOSYLATION
PLANT PROTEIN GLYCOSYLATION
topic ARABIDOPSIS
GLYCAN ARRAYS
GLYCAN FUNCTIONS
GLYCOSYL HYDROLASES
GLYCOSYLTRANSFERASES
N-GLYCOSYLATION
O-GLYCOSYLATION
PLANT PROTEIN GLYCOSYLATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.
Fil: Strasser, Richard. University of Natural Resources and Life Sciences; Suiza
Fil: Seifert, Georg. University of Natural Resources and Life Sciences; Suiza
Fil: Doblin, Monika S.. La Trobe University; Australia
Fil: Johnson, Kim L.. La Trobe University; Australia
Fil: Ruprecht, Colin. University of Natural Resources and Life Sciences; Suiza
Fil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; Suiza
Fil: Bacic, Antony. La Trobe University; Australia
Fil: Estevez, Jose Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
description Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.
publishDate 2021
dc.date.none.fl_str_mv 2021-02
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/11336/141685
Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-19
1664-462X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/141685
identifier_str_mv Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-19
1664-462X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.640919/full
info:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2021.640919
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
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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