Title (eng)
New insights into the N-glycomes of Dictyostelium species
Author
Daniel Malzl
Author
Chunsheng Jin
Author
Kristína Kianičková
Author
Iain B. H. Wilson
Author
Katharina Paschinger
Abstract (eng)
Dictyostelia are cellular slime molds, a group of Amoebozoa, that form multicellular fruiting bodies out of aggregating cells able of differentiating into resistant spore forms. In previous studies on Dictyostelium discoideum, it was demonstrated that their N-glycans, as in most eukaryotes, derive from the Glc3Man9GlcNAc2-PP-Dol precursor; however, unique glyco-epitopes, including intersecting GlcNAc, core α1,3-fucosylation, sulphation and methylphosphorylation, were detected. In the present study, we have examined the N-glycans of two other Dictyostelium species, D. purpureum, whose genome is also sequenced, and D. giganteum. The detailed glycomic analysis of their fruiting bodies was based on isomeric separation of the glycan structures by HPLC, followed by mass spectrometry in combination with enzymatic digests and chemical treatments. Two features absent from the 'model' dictyostelid D. discoideum were found: especially in D. purpureum, a long linear galactose arm β1,4-linked to the β1,4-N-acetylglucosamine on the 'lower' A-branch of its oligo-mannosylated structures could be identified. In contrast, neutral N-glycans with multiple fucose residues attached to terminal mannoses were found in D. giganteum. All three species have common modifications on their anionic N-glycans: while (methyl)phosphorylated residues are always associated with terminal mannose residues, the sulphation position differs. While D. discoideum has 6-sulphation of subterminal mannose residues, D. giganteum and D. purpureum may rather have 2-sulphation of core α1,6-mannose. Overall, we have discovered species-specific glycan variations and our data will contribute to future comparative and functional studies on these three species within the same genus.
Keywords (eng)
High-Mannose OligosaccharidesJack Bean MealLinked OligosaccharidesDevelopmental RegulationLysosomal-EnzymesDiscoideumGlycoproteinGlycansIdentificationGlycosylation
Type (eng)
Language
[eng]
Is in series
Title (eng)
BBA Advances
Volume
7
ISSN
2667-1603
Issued
2025
Number of pages
15
Publication
Elsevier
Date issued
2025
Access rights (eng)
Rights statement (eng)
© 2025 The Author(s)