Journal
FEBS JOURNAL
Volume 274, Issue 3, Pages 714-726Publisher
WILEY
DOI: 10.1111/j.1742-4658.2006.05615.x
Keywords
Ascaris; fucose; nematode; N-glycan; parasite; phosphorylcholine
Categories
Funding
- Austrian Science Fund FWF [P 18447] Funding Source: Medline
Ask authors/readers for more resources
In recent years, the glycoconjugates of many parasitic nematodes have attracted interest due to their immunogenic and immunomodulatory nature. Previous studies with the porcine roundworm parasite Ascaris suum have focused on its glycosphingolipids, which were found, in part, to be modified by phosphorylcholine. Using mass spectrometry and western blotting, we have now analyzed the peptide N-glycosidase A-released N-glycans of adults of this species. The presence of hybrid bi- and triantennary N-glycans, some modified by core alpha 1,6-fucose and peripheral phosphorylcholine, was demonstrated by LC/electrospray ionization (ESI)-Q-TOF-MS/MS, as was the presence of paucimannosidic N-glycans, some of which carry core alpha 1,3-fucose, and oligomannosidic oligosaccharides. Western blotting verified the presence of protein-bound phosphorylcholine and core alpha 1,3-fucose, whereas glycosyltransferase assays showed the presence of core alpha 1,6-fucosyltransferase and Lewis-type alpha 1,3-fucosyltransferase activities. Although, the unusual tri- and tetrafucosylated glycans found in the model nematode Caenorhabditis elegans were not found, the vast majority of the N-glycans found in A. suum represent a subset of those found in C. elegans; thus, our data demonstrate that the latter is an interesting glycobiological model for parasitic nematodes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available