Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation

Autores
Chang, Lan Yi; Teppa, Roxana Elin; Noel, Maxence; Gilormini, Pierre André; Decloquement, Mathieu; Lion, Cédric; Biot, Christophe; Mir, Anne Marie; Cogez, Virginie; Delannoy, Philippe; Khoo, Kay Hooi; Petit, Daniel; Guérardel, Yann; Harduin Lepers, Anne
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The mammalian mono-α2,8-sialyltransferase ST8Sia VI has been shown to catalyze the transfer of a unique sialic acid residues onto core 1 O-glycans leading to the formation of di-sialylated O-glycosylproteins and to a lesser extent to diSia motifs onto glycolipids like GD1a. Previous studies also reported the identification of an orthologue of the ST8SIA6 gene in the zebrafish genome. Trying to get insights into the biosynthesis and function of the oligo-sialylated glycoproteins during zebrafish development, we cloned and studied this fish α2,8-sialyltransferase homologue. In situ hybridization experiments demonstrate that expression of this gene is always detectable during zebrafish development both in the central nervous system and in non-neuronal tissues. Intriguingly, using biochemical approaches and the newly developed in vitro MicroPlate Sialyltransferase Assay (MPSA), we found that the zebrafish recombinant enzyme does not synthetize diSia motifs on glycoproteins or glycolipids as the human homologue does. Using comparative genomics and molecular phylogeny approaches, we show in this work that the human ST8Sia VI orthologue has disappeared in the ray-finned fish and that the homologue described in fish correspond to a new subfamily of α2,8-sialyltransferase named ST8Sia VIII that was not maintained in Chondrichtyes and Sarcopterygii.
Fil: Chang, Lan Yi. Universite Lille; Francia. Academia Sinica. Institute Of Biological Chemistry; República de China
Fil: Teppa, Roxana Elin. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Noel, Maxence. Universite Lille; Francia
Fil: Gilormini, Pierre André. Universite Lille; Francia
Fil: Decloquement, Mathieu. Universite Lille; Francia
Fil: Lion, Cédric. Universite Lille; Francia
Fil: Biot, Christophe. Universite Lille; Francia
Fil: Mir, Anne Marie. Universite Lille; Francia
Fil: Cogez, Virginie. Universite Lille; Francia
Fil: Delannoy, Philippe. Universite Lille; Francia
Fil: Khoo, Kay Hooi. Academia Sinica. Institute Of Biological Chemistry; República de China
Fil: Petit, Daniel. Universite de Limoges; Francia
Fil: Guérardel, Yann. Universite Lille; Francia
Fil: Harduin Lepers, Anne. Universite Lille; Francia
Materia
MONO-ALPHA-2,8-SIALYLTRANSFERASES
DISIA MOTIFS
EVOLUTION
FUNCTIONAL GENOMICS
ST8SIA
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:11336/105264
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/105264
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylationChang, Lan YiTeppa, Roxana ElinNoel, MaxenceGilormini, Pierre AndréDecloquement, MathieuLion, CédricBiot, ChristopheMir, Anne MarieCogez, VirginieDelannoy, PhilippeKhoo, Kay HooiPetit, DanielGuérardel, YannHarduin Lepers, AnneMONO-ALPHA-2,8-SIALYLTRANSFERASESDISIA MOTIFSEVOLUTIONFUNCTIONAL GENOMICSST8SIAhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The mammalian mono-α2,8-sialyltransferase ST8Sia VI has been shown to catalyze the transfer of a unique sialic acid residues onto core 1 O-glycans leading to the formation of di-sialylated O-glycosylproteins and to a lesser extent to diSia motifs onto glycolipids like GD1a. Previous studies also reported the identification of an orthologue of the ST8SIA6 gene in the zebrafish genome. Trying to get insights into the biosynthesis and function of the oligo-sialylated glycoproteins during zebrafish development, we cloned and studied this fish α2,8-sialyltransferase homologue. In situ hybridization experiments demonstrate that expression of this gene is always detectable during zebrafish development both in the central nervous system and in non-neuronal tissues. Intriguingly, using biochemical approaches and the newly developed in vitro MicroPlate Sialyltransferase Assay (MPSA), we found that the zebrafish recombinant enzyme does not synthetize diSia motifs on glycoproteins or glycolipids as the human homologue does. Using comparative genomics and molecular phylogeny approaches, we show in this work that the human ST8Sia VI orthologue has disappeared in the ray-finned fish and that the homologue described in fish correspond to a new subfamily of α2,8-sialyltransferase named ST8Sia VIII that was not maintained in Chondrichtyes and Sarcopterygii.Fil: Chang, Lan Yi. Universite Lille; Francia. Academia Sinica. Institute Of Biological Chemistry; República de ChinaFil: Teppa, Roxana Elin. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Noel, Maxence. Universite Lille; FranciaFil: Gilormini, Pierre André. Universite Lille; FranciaFil: Decloquement, Mathieu. Universite Lille; FranciaFil: Lion, Cédric. Universite Lille; FranciaFil: Biot, Christophe. Universite Lille; FranciaFil: Mir, Anne Marie. Universite Lille; FranciaFil: Cogez, Virginie. Universite Lille; FranciaFil: Delannoy, Philippe. Universite Lille; FranciaFil: Khoo, Kay Hooi. Academia Sinica. Institute Of Biological Chemistry; República de ChinaFil: Petit, Daniel. Universite de Limoges; FranciaFil: Guérardel, Yann. Universite Lille; FranciaFil: Harduin Lepers, Anne. Universite Lille; FranciaMDPI2019-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/105264Chang, Lan Yi; Teppa, Roxana Elin; Noel, Maxence; Gilormini, Pierre André; Decloquement, Mathieu; et al.; Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation; MDPI; International Journal of Molecular Sciences; 20; 3; 1-2019; 1-211422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/ijms20030622info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/20/3/622info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:50:02Zoai:ri.conicet.gov.ar:11336/105264instacron: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 09:50:02.895CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
title Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
spellingShingle Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
Chang, Lan Yi
MONO-ALPHA-2,8-SIALYLTRANSFERASES
DISIA MOTIFS
EVOLUTION
FUNCTIONAL GENOMICS
ST8SIA
title_short Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
title_full Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
title_fullStr Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
title_full_unstemmed Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
title_sort Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation
dc.creator.none.fl_str_mv Chang, Lan Yi
Teppa, Roxana Elin
Noel, Maxence
Gilormini, Pierre André
Decloquement, Mathieu
Lion, Cédric
Biot, Christophe
Mir, Anne Marie
Cogez, Virginie
Delannoy, Philippe
Khoo, Kay Hooi
Petit, Daniel
Guérardel, Yann
Harduin Lepers, Anne
author Chang, Lan Yi
author_facet Chang, Lan Yi
Teppa, Roxana Elin
Noel, Maxence
Gilormini, Pierre André
Decloquement, Mathieu
Lion, Cédric
Biot, Christophe
Mir, Anne Marie
Cogez, Virginie
Delannoy, Philippe
Khoo, Kay Hooi
Petit, Daniel
Guérardel, Yann
Harduin Lepers, Anne
author_role author
author2 Teppa, Roxana Elin
Noel, Maxence
Gilormini, Pierre André
Decloquement, Mathieu
Lion, Cédric
Biot, Christophe
Mir, Anne Marie
Cogez, Virginie
Delannoy, Philippe
Khoo, Kay Hooi
Petit, Daniel
Guérardel, Yann
Harduin Lepers, Anne
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv MONO-ALPHA-2,8-SIALYLTRANSFERASES
DISIA MOTIFS
EVOLUTION
FUNCTIONAL GENOMICS
ST8SIA
topic MONO-ALPHA-2,8-SIALYLTRANSFERASES
DISIA MOTIFS
EVOLUTION
FUNCTIONAL GENOMICS
ST8SIA
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The mammalian mono-α2,8-sialyltransferase ST8Sia VI has been shown to catalyze the transfer of a unique sialic acid residues onto core 1 O-glycans leading to the formation of di-sialylated O-glycosylproteins and to a lesser extent to diSia motifs onto glycolipids like GD1a. Previous studies also reported the identification of an orthologue of the ST8SIA6 gene in the zebrafish genome. Trying to get insights into the biosynthesis and function of the oligo-sialylated glycoproteins during zebrafish development, we cloned and studied this fish α2,8-sialyltransferase homologue. In situ hybridization experiments demonstrate that expression of this gene is always detectable during zebrafish development both in the central nervous system and in non-neuronal tissues. Intriguingly, using biochemical approaches and the newly developed in vitro MicroPlate Sialyltransferase Assay (MPSA), we found that the zebrafish recombinant enzyme does not synthetize diSia motifs on glycoproteins or glycolipids as the human homologue does. Using comparative genomics and molecular phylogeny approaches, we show in this work that the human ST8Sia VI orthologue has disappeared in the ray-finned fish and that the homologue described in fish correspond to a new subfamily of α2,8-sialyltransferase named ST8Sia VIII that was not maintained in Chondrichtyes and Sarcopterygii.
Fil: Chang, Lan Yi. Universite Lille; Francia. Academia Sinica. Institute Of Biological Chemistry; República de China
Fil: Teppa, Roxana Elin. Centre National de la Recherche Scientifique; Francia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Noel, Maxence. Universite Lille; Francia
Fil: Gilormini, Pierre André. Universite Lille; Francia
Fil: Decloquement, Mathieu. Universite Lille; Francia
Fil: Lion, Cédric. Universite Lille; Francia
Fil: Biot, Christophe. Universite Lille; Francia
Fil: Mir, Anne Marie. Universite Lille; Francia
Fil: Cogez, Virginie. Universite Lille; Francia
Fil: Delannoy, Philippe. Universite Lille; Francia
Fil: Khoo, Kay Hooi. Academia Sinica. Institute Of Biological Chemistry; República de China
Fil: Petit, Daniel. Universite de Limoges; Francia
Fil: Guérardel, Yann. Universite Lille; Francia
Fil: Harduin Lepers, Anne. Universite Lille; Francia
description The mammalian mono-α2,8-sialyltransferase ST8Sia VI has been shown to catalyze the transfer of a unique sialic acid residues onto core 1 O-glycans leading to the formation of di-sialylated O-glycosylproteins and to a lesser extent to diSia motifs onto glycolipids like GD1a. Previous studies also reported the identification of an orthologue of the ST8SIA6 gene in the zebrafish genome. Trying to get insights into the biosynthesis and function of the oligo-sialylated glycoproteins during zebrafish development, we cloned and studied this fish α2,8-sialyltransferase homologue. In situ hybridization experiments demonstrate that expression of this gene is always detectable during zebrafish development both in the central nervous system and in non-neuronal tissues. Intriguingly, using biochemical approaches and the newly developed in vitro MicroPlate Sialyltransferase Assay (MPSA), we found that the zebrafish recombinant enzyme does not synthetize diSia motifs on glycoproteins or glycolipids as the human homologue does. Using comparative genomics and molecular phylogeny approaches, we show in this work that the human ST8Sia VI orthologue has disappeared in the ray-finned fish and that the homologue described in fish correspond to a new subfamily of α2,8-sialyltransferase named ST8Sia VIII that was not maintained in Chondrichtyes and Sarcopterygii.
publishDate 2019
dc.date.none.fl_str_mv 2019-01
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/11336/105264
Chang, Lan Yi; Teppa, Roxana Elin; Noel, Maxence; Gilormini, Pierre André; Decloquement, Mathieu; et al.; Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation; MDPI; International Journal of Molecular Sciences; 20; 3; 1-2019; 1-21
1422-0067
CONICET Digital
CONICET
url http://hdl.handle.net/11336/105264
identifier_str_mv Chang, Lan Yi; Teppa, Roxana Elin; Noel, Maxence; Gilormini, Pierre André; Decloquement, Mathieu; et al.; Novel zebrafish mono-α2,8-sialyltransferase (ST8Sia VIII): An evolutionary perspective of α2,8-sialylation; MDPI; International Journal of Molecular Sciences; 20; 3; 1-2019; 1-21
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/doi/10.3390/ijms20030622
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/20/3/622
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 MDPI
publisher.none.fl_str_mv MDPI
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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