Integrative View of α2,3-Sialyltransferases (ST3Gal) Molecular and Functional Evolution in Deuterostomes: Significance of Lineage-Specific Losses

Petit, Daniel; Teppa, Elin; Mir, Anne-Marie; Vicogne, Dorothée; Thisse, Christine; Thisse, Bernard; Filloux, Cyril; Harduin-Lepers, Anne

doi:10.1093/molbev/msu395

Cited by 38 publications

(54 citation statements)

References 102 publications

(176 reference statements)

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“…As far as the st3gal genes are concerned, a first series of tandem duplication of an ancestral st3gal gene in proto-Metazoa stem led to the GR1 and GR2/GR3/GRx groups of α2,3-sialyltransferases before the Porifera emergence. As previously reported for α2,8-sialyltransferases [30], a second series of tandem duplication took place after the Porifera radiation that gave rise to the full diversity of α2,3-sialyltransferase groups, as confirmed using ancestral genome reconstruction data from Putnam et al [53,64]. This further indicates that the functional diversity of st3gal groups was acquired well before vertebrate divergence.…”

Section: When β-Galactoside α23/6-sialyltransferase Evolutionary supporting

confidence: 79%

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Teppa

Petit

Plechakova

et al. 2016

IJMS

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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 β-galactoside α2,3/6-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.

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Section: When β-Galactoside α23/6-sialyltransferase Evolutionary supporting

confidence: 79%

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Teppa

Petit

Plechakova

et al. 2016

IJMS

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“…For instance, multiple sialyltransferases are encoded by the genome of a cephalochordate (Branchiostoma belcheri); both N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid (Neu5Gc) were found to be expressed in a tissue-specific manner in this organism, while methylated 3-deoxy-Dglycero-D-galacto-2-nonulosonic acid (KDN; a non-acylated sialic acid) was found on ovary O-glycans [55]. In echinoderms, a number of α2,3-, α2,6and α2,8-sialyltransferase homologues, yet to be enzymatically characterised, occur in the sea urchin Strongylocentrotus purpuratus [56][57][58]; NeuAc and NeuGc are found in a number of echinoderm species, also in O-acetylated and O-sulphated forms. In starfish and sea cucumbers, a large percentage of these sialic acids are additionally methylated at O-8, whereas in other echinoderms this position can be sulphated [59,60].…”

Section: Sialic Acidsmentioning

confidence: 97%

Anionic and zwitterionic moieties as widespread glycan modifications in non-vertebrates

Paschinger

Wilson

2019

Glycoconj J

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Glycan structures in non-vertebrates are highly variable; it can be assumed that this is a product of evolution and speciation, not that it is just a random event. However, in animals and protists, there is a relatively limited repertoire of around ten monosaccharide building blocks, most of which are neutral in terms of charge. While two monosaccharide types in eukaryotes (hexuronic and sialic acids) are anionic, there are a number of organic or inorganic modifications of glycans such as sulphate, pyruvate, phosphate, phosphorylcholine, phosphoethanolamine and aminoethylphosphonate that also confer a 'charged' nature (either anionic or zwitterionic) to glycoconjugate structures. These alter the physicochemical properties of the glycans to which they are attached, change their ionisation when analysing them by mass spectrometry and result in different interactions with protein receptors. Here, we focus on N-glycans carrying anionic and zwitterionic modifications in protists and invertebrates, but make some reference to O-glycans, glycolipids and glycosaminoglycans which also contain such moieties. The conclusion is that 'charged' glycoconjugates are a widespread, but easily overlooked, feature of 'lower' organisms.

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“…Synthesis of polySia is catalyzed by two polysialyltransferases (polySTs), designated ST8Sia II (STX) and ST8Sia IV (PST). The finding that polyST gene "knock-down" experiments negates events associated with tumor cell dissemination indicates that polySTs are validated targets for potential drug therapies [8][9][10][11][12][13]. It is also known that cytidine monophosphate (CMP)-sialic acid (CMP-Sia), the activated nucleotide sugar of N-acetylneuraminic acid (Neu5Ac; Sia) [14][15][16][17][18][19], is required by the polySTs for biosynthesis of polySia [9,13,20,21].…”

Section: Introductionmentioning

confidence: 99%

Molecular Interactions of the Polysialytransferase Domain (PSTD) in ST8Sia IV with CMP-Sialic Acid and Polysialic Acid Required for Polysialylation of the Neural Cell Adhesion Molecule Proteins: An NMR Study

Liao

Lü

et al. 2020

IJMS

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Polysialic acid (polySia) is an unusual glycan that posttranslational modifies neural cell adhesion molecule (NCAM) proteins in mammalian cells. The up-regulated expression of polySia-NCAM is associated with tumor progression in many metastatic human cancers and in neurocognitive processes. Two members of the ST8Sia family of α2,8-polysialyltransferases (polySTs), ST8Sia II (STX) and ST8Sia IV (PST) both catalyze synthesis of polySia when activated cytidine monophosphate(CMP)-Sialic acid (CMP-Sia) is translocate into the lumen of the Golgi apparatus. Two key polybasic domains in the polySTs, the polybasic region (PBR) and the polysialyltransferase domain (PSTD) areessential forpolysialylation of the NCAM proteins. However, the precise molecular details to describe the interactions required for polysialylation remain unknown. In this study, we hypothesize that PSTD interacts with both CMP-Sia and polySia to catalyze polysialylation of the NCAM proteins. To test this hypothesis, we synthesized a 35-amino acid-PSTD peptide derived from the ST8Sia IV gene sequence and used it to study its interaction with CMP-Sia, and polySia. Our results showed for the PSTD-CMP-Sia interaction, the largest chemical-shift perturbations (CSP) were in amino acid residues V251 to A254 in the short H1 helix, located near the N-terminus of PSTD. However, larger CSP values for the PSTD-polySia interaction were observed in amino acid residues R259 to T270 in the long H2 helix. These differences suggest that CMP-Sia preferentially binds to the domain between the short H1 helix and the longer H2 helix. In contrast, polySia was principally bound to the long H2 helix of PSTD. For the PSTD-polySia interaction, a significant decrease in peak intensity was observed in the 20 amino acid residues located between the N-and C-termini of the long H2 helix in PSTD, suggesting a slower motion in these residues when polySia bound to PSTD. Specific features of the interactions between PSTD-CMP-Sia, and PSTD-polySia were further confirmed by comparing their 800 MHz-derived HSQC spectra with that of PSTD-Sia, PSTD-TriSia (DP 3) and PSTD-polySia. Based on the interactions between PSTD-CMP-Sia, PSTD-polySia, PBR-NCAM and PSTD-PBR, these findingsprovide a greater understanding of the molecular mechanisms underlying polySia-NCAM polysialylation, and thus provides a new perspective for translational pharmacological applications and development by targeting the two polysialyltransferases.

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Integrative View of α2,3-Sialyltransferases (ST3Gal) Molecular and Functional Evolution in Deuterostomes: Significance of Lineage-Specific Losses

Cited by 38 publications

References 102 publications

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Anionic and zwitterionic moieties as widespread glycan modifications in non-vertebrates

Molecular Interactions of the Polysialytransferase Domain (PSTD) in ST8Sia IV with CMP-Sialic Acid and Polysialic Acid Required for Polysialylation of the Neural Cell Adhesion Molecule Proteins: An NMR Study

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