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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, Elin; Noel, Maxence; Gilormini, Pierre-André; Decloquement, Mathieu; Lion, Cedric; Biot, Christophe; Mir, Anne-Marie; Cogez, Virginie; Delannoy, Philippe; Khoo, Kay-Hooi; Petit, Daniel; Guerardel, Yann; Harduin Lepers, Anne
Contributors: Université de Lille; CNRS; Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 UGSF; Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576; Academia Sinica; Biologie Computationnelle et Quantitative = Laboratory of Computational and Quantitative Biology LCQB; Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 UGSF; PEIRENE PEIRENE
Publisher Information: MDPI
Publication Year: 2020
Collection: LillOA (Lille Open Archive - Université de Lille)
Subject Terms: mono-α2,8-sialyltransferases; diSia motifs; evolution; ST8Sia; functional genomics
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. ; 20;3
Document Type: article in journal/newspaper
File Description: application/rdf+xml; charset=utf-8; application/octet-stream
Language: English
Relation: International Journal of Molecular Sciences; IJMS; http://hdl.handle.net/20.500.12210/33844
Availability: https://hdl.handle.net/20.500.12210/33844
Rights: Attribution 3.0 United States ; info:eu-repo/semantics/openAccess
Accession Number: edsbas.8FE3D65B
Database: BASE