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Novel O-linked methylated glycan antigens decorate secreted immunodominant glycoproteins from the intestinal nematode Heligmosomoides polygyrus

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Original languageEnglish
Pages (from-to)157-170
Number of pages14
JournalInternational Journal For Parasitology
Issue number3
Early online date12 Dec 2015
Publication statusPublished - Mar 2016


Glycan molecules from helminth parasites have been associated with diverse biological functions ranging from interactions with neighbouring host cell populations to down-modulation of specific host immunity. Glycoproteins secreted by the intestinal nematode Heligmosomoides polygyrus are of particular interest as the excretory–secretory products (termed HES) of this parasite contain both heat-labile and heat-stable components with immunomodulatory effects. We used MALDI-TOF-MS and LC–MS/MS to analyse the repertoire of HES N- and O-linked glycans released by PNGase A and F, β-elimination and hydrazinolysis revealing a broad range of structures including novel methylhexose- and methylfucose-containing glycans. Monoclonal antibodies to two immunodominant glycans of H. polygyrus, previously designated Glycans A and B, were found to react by glycan array analysis to a methyl-hexose-rich fraction and to a sulphated LacDiNAc (LDN; GalNAcβ1–4GlcNAc) structure, respectively. We also analysed the glycan repertoire of a major HES glycoprotein, VAL-2, which contains many glycan structures present in HES including Glycan A. However, it was found that this set of glycans is not responsible for the heat-stable immunomodulatory properties of HES, as revealed by the inability of VAL-2 to inhibit allergic lung inflammation. Taken together, these studies reveal that H. polygyrus secretes a diverse range of antigenic glycoconjugates, and provides a framework to explore the biological and immunomodulatory roles they may play within the mammalian host.

    Research areas

  • Heligmosomoides polygyrus, Antibody, Carbohydrate, Excretory-secretory product, Mass spectrometry, Nematode

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