Site- and Structure-Specific Characterization of Glycoproteins of H11: Potent Vaccine Candidates against Parasitic Worm Haemonchus

ABSTRACT: Parasitic worms (helminths) represent a major class of human and animal pathogens that impact agriculture and economies worldwide. Over the past few decades, Mass spectrometry (MS)-based glycomics studies have revealed that helminths possess an abundance of complex and unique glycoconjugates that interact with both the innate and adaptive arms of immunity in definitive and intermediate hosts. Despite these advancements, comprehensive characterization of the intact glycoproteome in helminth species remains a significant challenge. Here, we performed site- and structure-specific N-glycoproteins analyses to investigate an important vaccine component – termed H11 antigen derived from pathogenic parasite Haemonchus contortus. We identified seven glycosylated aminopeptidases carrying 19 N-glycosylation sites corresponding to 31 distinct N-glycan structures. Among these, 13 N-glycopeptides were significantly enriched by H11-induced protective IgG antibodies. Our analyses revealed a high degree of structural heterogeneity and abundant core fucosylation among the identified glycopeptides. Molecular docking showed that these IgG-recognized N-glycopeptides are located on the surface and around the channel through which substrates enter the active site of the aminopeptidases, suggesting their potential as antigenic epitopes. Our work provides the comprehensive glycoprotein profiling in an economically important parasitic worm, with important implications for the design of vaccines against those parasites

INSTRUMENT(S):

ORGANISM(S): Haemonchus Contortus (barber Pole Worm)

SUBMITTER: Chunqun Wang  

LAB HEAD: Chunqun Wang

PROVIDER: PXD068910 | Pride | 2025-12-17

REPOSITORIES: Pride