N-Glycome and N-Glycoproteome of a Hematophagous Parasitic Nematode Haemonchus

N-glycosylation is a physiologically vital post-translational modification of proteins in eukaryotic organisms. Initial work on Haemonchus contortus – an economically-important blood-sucking nematode of ruminants with a broad geographical distribution – has shown that the parasite harbors N-glycans with exclusive core chitobiose modifications, and severel immunogenic proteins (e.g., amino- and metallo-peptidases) in the adult worms are N-glycosylated. However, an informative atlas of N-glycosylation in H. contortus is not yet available. Herein, we report a total of 291 N-glycosylated proteins with 425 sites in this parasite. Functional analyses of glycoproteome revealed significant enrichment of the peptidase families (e.g., peptidase C1 and M1), many of which are potential vaccine targets. Besides, the glycan-rich conjugates are distributed primarily in the intestine and gonads of the adult worms. These data, taken together, provide a comprehensive insight into the N-glycosylation of a prevalent parasitic nematode, while underlining its significance for the infection and prophylaxis.