Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)

Autores
Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.
Fil: Teppa, Roxana Elin. 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
Fil: Petit, Daniel. Université de Limoges; Francia
Fil: Plechakova, Olga. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Cogez, Virginie. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Harduin-Lepers, Anne. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Materia
EVOLUTION
FUNCTIONAL GENOMICS
MOLECULAR PHYLOGENY
SIALIC ACID
SIALYLTRANSFERASES
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:11336/84338
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)Teppa, Roxana ElinPetit, DanielPlechakova, OlgaCogez, VirginieHarduin-Lepers, AnneEVOLUTIONFUNCTIONAL GENOMICSMOLECULAR PHYLOGENYSIALIC ACIDSIALYLTRANSFERASEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.Fil: Teppa, Roxana Elin. 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; ArgentinaFil: Petit, Daniel. Université de Limoges; FranciaFil: Plechakova, Olga. Universite Lille; Francia. Centre National de la Recherche Scientifique; FranciaFil: Cogez, Virginie. Universite Lille; Francia. Centre National de la Recherche Scientifique; FranciaFil: Harduin-Lepers, Anne. Universite Lille; Francia. Centre National de la Recherche Scientifique; FranciaMolecular Diversity Preservation International2016-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84338Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne; Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal); Molecular Diversity Preservation International; International Journal of Molecular Sciences; 17; 8; 8-20161422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/17/8/1286/htmlinfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms17081286info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-17T11:39:55Zoai:ri.conicet.gov.ar:11336/84338instacron: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:34982025-09-17 11:39:55.331CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
title Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
spellingShingle Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
Teppa, Roxana Elin
EVOLUTION
FUNCTIONAL GENOMICS
MOLECULAR PHYLOGENY
SIALIC ACID
SIALYLTRANSFERASES
title_short Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
title_full Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
title_fullStr Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
title_full_unstemmed Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
title_sort Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal)
dc.creator.none.fl_str_mv Teppa, Roxana Elin
Petit, Daniel
Plechakova, Olga
Cogez, Virginie
Harduin-Lepers, Anne
author Teppa, Roxana Elin
author_facet Teppa, Roxana Elin
Petit, Daniel
Plechakova, Olga
Cogez, Virginie
Harduin-Lepers, Anne
author_role author
author2 Petit, Daniel
Plechakova, Olga
Cogez, Virginie
Harduin-Lepers, Anne
author2_role author
author
author
author
dc.subject.none.fl_str_mv EVOLUTION
FUNCTIONAL GENOMICS
MOLECULAR PHYLOGENY
SIALIC ACID
SIALYLTRANSFERASES
topic EVOLUTION
FUNCTIONAL GENOMICS
MOLECULAR PHYLOGENY
SIALIC ACID
SIALYLTRANSFERASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.
Fil: Teppa, Roxana Elin. 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
Fil: Petit, Daniel. Université de Limoges; Francia
Fil: Plechakova, Olga. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Cogez, Virginie. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
Fil: Harduin-Lepers, Anne. Universite Lille; Francia. Centre National de la Recherche Scientifique; Francia
description Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.
publishDate 2016
dc.date.none.fl_str_mv 2016-08
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/11336/84338
Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne; Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal); Molecular Diversity Preservation International; International Journal of Molecular Sciences; 17; 8; 8-2016
1422-0067
CONICET Digital
CONICET
url http://hdl.handle.net/11336/84338
identifier_str_mv Teppa, Roxana Elin; Petit, Daniel; Plechakova, Olga; Cogez, Virginie; Harduin-Lepers, Anne; Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal); Molecular Diversity Preservation International; International Journal of Molecular Sciences; 17; 8; 8-2016
1422-0067
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1422-0067/17/8/1286/html
info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms17081286
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 Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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 13.001348

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