Evidence map›Paper›PMID 25534026›Full record

ArticleMolecular biology and evolution2015

Integrative view of α2,3-sialyltransferases (ST3Gal) molecular and functional evolution in deuterostomes: significance of lineage-specific losses.

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

Open access · hybridAbstract read
In one paragraph

Article in Molecular biology and evolution, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 41 citations in OpenAlex.

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  11. Harnessing the sponge microbiome for industrial biocatalysts.Applied microbiology and biotechnology · 2020
    Review
  12. Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020
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  13. Article
  14. Review
  15. Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective.International journal of molecular sciences · 2020
    Article
  16. Article
  17. Review
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 6 institutions in 3 countries.

Daniel PetitINRA, UMR 1061, Unité Génétique Moléculaire Animale, F-87060 Limoges Cedex, France Université de Limoges, UMR 1061, Unité Génétique Moléculaire Animale, 123 avenue Albert Thomas, F-87060 Limoges Cedex, France.
Elin TeppaBioinformatics Unit, Fundación Instituto Leloir, Buenos Aires, Argentina.
Anne-Marie MirLaboratoire de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Université Lille Nord de France, Lille1, Villeneuve d'Ascq, France.
Dorothée VicogneLaboratoire de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Université Lille Nord de France, Lille1, Villeneuve d'Ascq, France.
Christine ThisseDepartment of Cell Biology, School of Medicine, University of Virginia.
Bernard ThisseDepartment of Cell Biology, School of Medicine, University of Virginia.
Cyril FillouxINRA, UMR 1061, Unité Génétique Moléculaire Animale, F-87060 Limoges Cedex, France Université de Limoges, UMR 1061, Unité Génétique Moléculaire Animale, 123 avenue Albert Thomas, F-87060 Limoges Cedex, France.
Anne Harduin-LepersLaboratoire de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, Université Lille Nord de France, Lille1, Villeneuve d'Ascq, France anne.harduin@univ-lille1.fr.
Université de Limoges · FRUniversity of Virginia · USCentre National de la Recherche Scientifique · FRFundación Instituto Leloir · ARUnité de Glycobiologie Structurale et Fonctionnelle · FRUniversité Lille Nord de France · FR

Funding

GENOME RESOURCES FOR MODEL AMPHIBIANSR24RR016344 · NCRR · UNIVERSITY OF KENTUCKY · PI VOSS, STEPHEN RANDAL · 2002 to 2011
$3.5M
NCRR NIH HHS 5R24RR016344NCRR NIH HHS R24 RR016344
6 · The paper itself

Abstract

Sialyltransferases are responsible for the synthesis of a diverse range of sialoglycoconjugates predicted to be pivotal to deuterostomes' evolution. In this work, we reconstructed the evolutionary history of the metazoan α2,3-sialyltransferases family (ST3Gal), a subset of sialyltransferases encompassing six subfamilies (ST3Gal I-ST3Gal VI) functionally characterized in mammals. Exploration of genomic and expressed sequence tag databases and search of conserved sialylmotifs led to the identification of a large data set of st3gal-related gene sequences. Molecular phylogeny and large scale sequence similarity network analysis identified four new vertebrate subfamilies called ST3Gal III-r, ST3Gal VII, ST3Gal VIII, and ST3Gal IX. To address the issue of the origin and evolutionary relationships of the st3gal-related genes, we performed comparative syntenic mapping of st3gal gene loci combined to ancestral genome reconstruction. The ten vertebrate ST3Gal subfamilies originated from genome duplication events at the base of vertebrates and are organized in three distinct and ancient groups of genes predating the early deuterostomes. Inferring st3gal gene family history identified also several lineage-specific gene losses, the significance of which was explored in a functional context. Toward this aim, spatiotemporal distribution of st3gal genes was analyzed in zebrafish and bovine tissues. In addition, molecular evolutionary analyses using specificity determining position and coevolved amino acid predictions led to the identification of amino acid residues with potential implication in functional divergence of vertebrate ST3Gal. We propose a detailed scenario of the evolutionary relationships of st3gal genes coupled to a conceptual framework of the evolution of ST3Gal functions.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsbeta-Galactoside alpha-2,3-SialyltransferaseChordataEchinodermataMolecular Sequence DataPhylogenySialyltransferasesVertebratesbeta-Galactoside alpha-2,3-SialyltransferaseSialyltransferasescoevolved amino acidevolution ratesgenomicsglycobiologymolecular evolutionmolecular modelingphylogeneticsspecificity determining positionzebrafishβ-galactoside α2,3-sialyltransferases

Identifiers

PMID25534026
PMCPMC4379398
OpenAlexW2131695824

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.