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Open AccessArticle

Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective

Institute of Reproductive Biology, Leibniz Institute for Farm Animal Biology (FBN), Wilhelm-Stahl-Allee 2, 18196 Dummerstorf, Germany
Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France
Institute of Genome Biology Leibniz Institute for Farm Animal Biology (FBN), Wilhelm-Stahl-Allee 2, 18196 Dummerstorf, Germany
Glycosylation et Différenciation Cellulaire, EA 7500, Laboratoire PEIRENE, Université de Limoges, 123 Avenue Albert Thomas, 87060 Limoges CEDEX, France
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(2), 513;
Received: 29 November 2019 / Revised: 6 January 2020 / Accepted: 10 January 2020 / Published: 14 January 2020
We identified and analyzed α2,8-sialyltransferases sequences among 71 ray-finned fish species to provide the first comprehensive view of the Teleost ST8Sia repertoire. This repertoire expanded over the course of Vertebrate evolution and was primarily shaped by the whole genome events R1 and R2, but not by the Teleost-specific R3. We showed that duplicated st8sia genes like st8sia7, st8sia8, and st8sia9 have disappeared from Tetrapods, whereas their orthologues were maintained in Teleosts. Furthermore, several fish species specific genome duplications account for the presence of multiple poly-α2,8-sialyltransferases in the Salmonidae (ST8Sia II-r1 and ST8Sia II-r2) and in Cyprinus carpio (ST8Sia IV-r1 and ST8Sia IV-r2). Paralogy and synteny analyses provided more relevant and solid information that enabled us to reconstruct the evolutionary history of st8sia genes in fish genomes. Our data also indicated that, while the mammalian ST8Sia family is comprised of six subfamilies forming di-, oligo-, or polymers of α2,8-linked sialic acids, the fish ST8Sia family, amounting to a total of 10 genes in fish, appears to be much more diverse and shows a patchy distribution among fish species. A focus on Salmonidae showed that (i) the two copies of st8sia2 genes have overall contrasted tissue-specific expressions, with noticeable changes when compared with human co-orthologue, and that (ii) st8sia4 is weakly expressed. Multiple sequence alignments enabled us to detect changes in the conserved polysialyltransferase domain (PSTD) of the fish sequences that could account for variable enzymatic activities. These data provide the bases for further functional studies using recombinant enzymes. View Full-Text
Keywords: molecular phylogeny; α2,8-sialyltransferases; polySia motifs; evolution; ST8Sia; functional genomics molecular phylogeny; α2,8-sialyltransferases; polySia motifs; evolution; ST8Sia; functional genomics
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MDPI and ACS Style

Venuto, M.T.; Decloquement, M.; Martorell Ribera, J.; Noel, M.; Rebl, A.; Cogez, V.; Petit, D.; Galuska, S.P.; Harduin-Lepers, A. Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective. Int. J. Mol. Sci. 2020, 21, 513.

AMA Style

Venuto MT, Decloquement M, Martorell Ribera J, Noel M, Rebl A, Cogez V, Petit D, Galuska SP, Harduin-Lepers A. Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective. International Journal of Molecular Sciences. 2020; 21(2):513.

Chicago/Turabian Style

Venuto, Marzia T.; Decloquement, Mathieu; Martorell Ribera, Joan; Noel, Maxence; Rebl, Alexander; Cogez, Virginie; Petit, Daniel; Galuska, Sebastian P.; Harduin-Lepers, Anne. 2020. "Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective" Int. J. Mol. Sci. 21, no. 2: 513.

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