Increasing Complexity of the N-Glycome During Caenorhabditis Development.

Wilson IBH, Yan S, Jin C, Dutkiewicz Z, Rendić D, Palmberger D, Schnabel R, Paschinger K

Mol. Cell Proteomics 22 (3) 100505 [2023-03-00; online 2023-01-28]

Caenorhabditis elegans is a frequently employed genetic model organism and has been the object of a wide range of developmental, genetic, proteomic, and glycomic studies. Here, using an off-line MALDI-TOF-MS approach, we have analyzed the N-glycans of mixed embryos and liquid- or plate-grown L4 larvae. Of the over 200 different annotatable N-glycan structures, variations between the stages as well as the mode of cultivation were observed. While the embryonal N-glycome appears less complicated overall, the liquid- and plate-grown larvae differ especially in terms of methylation of bisecting fucose, α-galactosylation of mannose, and di-β-galactosylation of core α1,6-fucose. Furthermore, we analyzed the O-glycans by LC-electrospray ionization-MS following β-elimination; especially the embryonal O-glycomes included a set of phosphorylcholine-modified structures, previously not shown to exist in nematodes. However, the set of glycan structures cannot be clearly correlated with levels of glycosyltransferase transcripts in developmental RNA-Seq datasets, but there is an indication for coordinated expression of clusters of potential glycosylation-relevant genes. Thus, there are still questions to be answered in terms of how and why a simple nematode synthesizes such a diverse glycome.

Glycoproteomics and MS Proteomics [Collaborative]

PubMed 36717059

DOI 10.1016/j.mcpro.2023.100505

Crossref 10.1016/j.mcpro.2023.100505

mid: EMS170519
pmc: PMC7614267
pii: S1535-9476(23)00014-2

Publications 9.5.0