Vertebrate Alpha2,8-Sialyltransferases ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective
Auteur(s) :
Venuto, Marzia Tindara [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Decloquement, Mathieu [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Martorell Ribera, Joan [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Noel, Maxence [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Rebl, Alexander [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Cogez, Virginie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Petit, Daniel [Auteur]
Galuska, Sebastian Peter [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Leibniz Institute for Farm Animal Biology [FBN]
Decloquement, Mathieu [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Martorell Ribera, Joan [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Noel, Maxence [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Rebl, Alexander [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Cogez, Virginie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Petit, Daniel [Auteur]
Galuska, Sebastian Peter [Auteur]
Leibniz Institute for Farm Animal Biology [FBN]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Titre de la revue :
International Journal of Molecular Sciences
Nom court de la revue :
IJMS
Numéro :
21
Pagination :
513
Éditeur :
MDPI AG
Date de publication :
2020-01-14
ISSN :
1422-0067
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Régulation de la glycosylation terminale
Date de dépôt :
2020-06-26T11:57:09Z
2020-09-24T13:45:45Z
2020-09-24T13:45:45Z
Fichiers
- P20.03 Venuto et al 2020 IJMS.pdf
- Version éditeur
- Accès libre
- Accéder au document