Novel Zebrafish Mono-α2,8-sialyltransferase ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
Novel Zebrafish Mono-α2,8-sialyltransferase (ST8Sia VIII): An Evolutionary Perspective of α2,8-Sialylation
Auteur(s) :
Chang, Lan-Yi [Auteur]
Teppa, Elin [Auteur]
Noel, Maxence [Auteur]
Gilormini, Pierre-André [Auteur]
Decloquement, Mathieu [Auteur]
Lion, Cédric [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Biot, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Mir, Anne-Marie [Auteur]
Cogez, Virginie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Delannoy, Philippe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Khoo, Kay [Auteur]
Petit, Daniel [Auteur]
Guerardel, Yann [Auteur]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Teppa, Elin [Auteur]
Noel, Maxence [Auteur]
Gilormini, Pierre-André [Auteur]
Decloquement, Mathieu [Auteur]
Lion, Cédric [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Biot, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Mir, Anne-Marie [Auteur]
Cogez, Virginie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Delannoy, Philippe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Khoo, Kay [Auteur]
Petit, Daniel [Auteur]
Guerardel, Yann [Auteur]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Titre de la revue :
International Journal of Molecular Sciences
Nom court de la revue :
IJMS
Numéro :
20
Pagination :
622
Éditeur :
MDPI AG
Date de publication :
2019-01-31
ISSN :
1422-0067
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Régulation de la glycosylation terminale
Glycobiologie structurale des interactions hôtes-pathogènes
Glycobiologie structurale des interactions hôtes-pathogènes
Date de dépôt :
2020-12-07T10:23:48Z
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