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- W3153200310 abstract "N-glycosylation is a physiologically vital post-translational modification of proteins in eukaryotic organisms. Initial work on Haemonchus contortus - a blood-sucking nematode of ruminants with a broad geographical distribution - has shown that this parasite harbors N-glycans with exclusive chitobiose modifications. Besides, several immunogenic proteins (e.g., amino- and metallo-peptidases) are known to be N-glycosylated in adult worms. However, an informative atlas of N-glycosylation in H. contortus is not yet available. Herein, we report 291 N-glycosylated proteins with a total of 425 modification sites in the parasite. Among them, many peptidase families (e.g., peptidase C1 and M1) including potential vaccine targets were enriched. Notably, the glycan-rich conjugates are distributed primarily in the intestine and gonads of adult worms, and consequently hidden from the host's immune system. Collectively, these data provide a comprehensive atlas of N-glycosylation in a prevalent parasitic nematode while underlining its significance for infection, immunity and prevention." @default.
- W3153200310 created "2021-04-26" @default.
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- W3153200310 date "2021-01-01" @default.
- W3153200310 modified "2023-09-28" @default.
- W3153200310 title "N-glycome and N-glycoproteome of a hematophagous parasitic nematode Haemonchus" @default.
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- W3153200310 doi "https://doi.org/10.1016/j.csbj.2021.04.038" @default.
- W3153200310 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8113779" @default.
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