ArticleGlycobiology2018
The parasitic nematode Oesophagostomum dentatum synthesizes unusual glycosaminoglycan-like O-glycans.
Article in Glycobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Deciphering theBiomolecules · 2025Review
- Analysis of Caenorhabditis Protein Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The role of glycoconjugates as receptors for insecticidal proteins.FEMS microbiology reviews · 2023Review
- Increasing Complexity of the N-Glycome During Caenorhabditis Development.Molecular & cellular proteomics : MCP · 2023Article
- Negative-mode mass spectrometry in the analysis of invertebrate, fungal, and protist N-glycans.Mass spectrometry reviews · 2022Review
- Let's talk about sexes: sex-related N-glycosylation in ecologically important invertebrates.Glycoconjugate journal · 2020Review
- Anionic and zwitterionic moieties as widespread glycan modifications in non-vertebrates.Glycoconjugate journal · 2020Review
- Comparisons of N-glycans across invertebrate phyla.Parasitology · 2019Review
- Site-specific glycoproteomic characterization of ES-62: The major secreted product of the parasitic worm Acanthocheilonema viteae.Glycobiology · 2019Article
- Structures and functions of invertebrate glycosylation.Open biology · 2019Review
- N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
O-glycosylation is probably one of the most varied sets of post-translational modifications across all organisms, but amongst the most refractory to analyze. In animals, O-xylosylation of serine residues represents the first stage in the synthesis of glycosaminoglycans, whose repeat regions are generally analyzed as fragments resulting from enzymatic or chemical degradation, whereas their core regions can be isolated by β-elimination or endo-β-xylosidase digestion. In the present study, we show that hydrazinolysis can be employed for release of glycosaminoglycan-type oligosaccharides from nematodes prior to fluorescent labeling with 2-aminopyridine. While various [HexNAcHexA]nGal2Xyl oligosaccharides were isolated from the model organism Caenorhabditis elegans, more unusual glycosaminoglycan-type glycans were found to be present in the porcine parasite Oesophagostomum dentatum. In this case, as judged by MS/MS before and after hydrofluoric acid or β-galactosidase digestion, core sequences with extra galactose and phosphorylcholine residues were detected as [(±PC)HexNAcHexA]n(±PC)Galβ3-(±Galβ4)Galβ4Xyl. Thus, hydrazinolysis and fluorescent labeling can be combined to analyze unique forms of O-xylosylation, including new examples of zwitterionic glycan modifications.
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Registered trials
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