? 2016 by the authors; licensee MDPI, Basel, Switzerland.Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on ?-galactoside ?2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.
Teppa, R. E., Petit, D., Plechakova, O., Cogez, V., & Harduin-Lepers, A. (2016, August 9). Phylogenetic-derived insights into the evolution of sialylation in eukaryotes: Comprehensive analysis of vertebrate β-galactoside α2,3/6-sialyltransferases (ST3Gal and ST6Gal). International Journal of Molecular Sciences. MDPI AG. https://doi.org/10.3390/ijms17081286