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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
Authors: 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
Publisher Information: MDPI
Collection: CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
Subject Terms: MONO-ALPHA-2,8-SIALYLTRANSFERASES; DISIA MOTIFS; EVOLUTION; FUNCTIONAL GENOMICS; ST8SIA; https://purl.org/becyt/ford/1.6; https://purl.org/becyt/ford/1
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. ; 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 ...
Document Type: article in journal/newspaper
File Description: application/pdf
Language: English
Relation: info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/20/3/622; https://hdl.handle.net/11336/105264; CONICET Digital; CONICET
Availability: https://hdl.handle.net/11336/105264
Rights: info:eu-repo/semantics/openAccess ; https://creativecommons.org/licenses/by/2.5/ar/
Accession Number: edsbas.68F9CB56
Database: BASE