PUBLICATION
Novel Zebrafish Mono-α2,8-sialyltransferase (ST8Sia VIII): An Evolutionary Perspective of α2,8-Sialylation
- Authors
- Chang, L.Y., Teppa, E., Noel, M., Gilormini, P.A., Decloquement, M., Lion, C., Biot, C., Mir, A.M., Cogez, V., Delannoy, P., Khoo, K.H., Petit, D., Guérardel, Y., Harduin-Lepers, A.
- ID
- ZDB-PUB-190203-12
- Date
- 2019
- Source
- International Journal of Molecular Sciences 20(3): (Journal)
- Registered Authors
- Keywords
- ST8Sia, diSia motifs, evolution, functional genomics, mono-α2,8-sialyltransferases
- MeSH Terms
-
- Animals
- COS Cells
- Central Nervous System/metabolism
- Chlorocebus aethiops
- Computer Simulation
- Evolution, Molecular
- Gene Expression Regulation, Developmental
- Glycolipids/chemistry
- Glycoproteins/chemistry
- HEK293 Cells
- Humans
- Phylogeny
- Sequence Homology, Nucleic Acid
- Sialyltransferases/genetics*
- Sialyltransferases/metabolism*
- Substrate Specificity
- Tissue Distribution
- Zebrafish/genetics
- Zebrafish/growth & development*
- Zebrafish/metabolism
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism*
- PubMed
- 30709055 Full text @ Int. J. Mol. Sci.
Citation
Chang, L.Y., Teppa, E., Noel, M., Gilormini, P.A., Decloquement, M., Lion, C., Biot, C., Mir, A.M., Cogez, V., Delannoy, P., Khoo, K.H., Petit, D., Guérardel, Y., Harduin-Lepers, A. (2019) Novel Zebrafish Mono-α2,8-sialyltransferase (ST8Sia VIII): An Evolutionary Perspective of α2,8-Sialylation. International Journal of Molecular Sciences. 20(3).
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping