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N‐Glycan Complexity in Model and Parasitic Helminths
Author(s) -
Wilson Iain,
Eckmair Barbara,
Yan Shi,
Martini Francesca,
Paschinger Katharina
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.04256
Subject(s) - biology , glycan , caenorhabditis elegans , planarian , fasciola hepatica , zoology , helminths , microbiology and biotechnology , genetics , glycoprotein , gene , regeneration (biology)
Protein‐linked glycans are not only highly heterogenous within an organism, but also can differ highly between organisms. We have analysed N‐glycans from a range of invertebrates, including various members of two phyla: the Nematoda and the Platyhelminthes, including model organisms such as Caenorhabditis elegans and the planarian Dugesia japonica and parasites such as Echinococcus granulosus, Oesophagostomum dentatum, Dirofilaria immitis and Trichuris suis. Although the most abundant N‐glycans are pauci‐ and oligomannosidic structures, the inter‐species variability is seen with the modifications of the core mannosylchitobiosyl region and the antennae. In some species, unusual galactosylated substitutions of the core never observed in higher animals are observed, whereas up to four antennae are detected in others. A trend towards antennal substitutions may be discerned in parasitic species: this may reflect the evolutionary importance of interactions of the mammalian innate and adaptive immune systems with exposed epitopes on glycans of the parasite surfaces or excretory/secretory products, which also can modulate host responses to helminth infections. Thereby, we employ not just glycan analyses based on mass spectrometry, but increasingly look towards glycan arrays as a tool to determine the structural and functional aspects of these fascinating post‐translational modifications.