Glycosylation of Caenorhabditis elegans III

The model organism, Caenorhabditis elegans, is much studied at the genetic level; however, its glycosylation – a set of key modifications of all cell surfaces – is still poorly understood. Recent data from this and other laboratories suggest that the carbohydrates covalently-bound to nematode glycoproteins share some basic features with those found in mammals, but have some novel decorations. In particular, the presence of asparagine-linked glycan structures with up to four fucose residues and two O-methyl substitutions, as well as phosphorylcholine, is highly intriguing. Some of these features are shared, at least in part, by parasitic nematodes and so Caenorhabditis elegans is potentially a useful model for developing novel strategies in the study of these types of oligosaccharides with potential benefits in combatting nematode parasites. In the proposed study, it is intended to continue a long-term study on the biosynthesis and structure of the N-glycans of Caenorhabditis. In particular, using glycan analysis of double glycomutants, assays of a novel fucosyltransferase and the use of a chemical probe for fucosylation as well as a comparison with nematode parasites of plants, a variety of biochemical and analytical tools will be employed so as to uncover aspects of the molecular basis for multiple fucosylation events in the model nematode; the potential implications are to identify enzymes generating unusual glycan structures which in parasitic organisms may play roles in host-parasite interactions.