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Resources » Paper

Paschinger K et al. (2023) J Biol Chem "N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase."

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  • Comments on Paschinger K et al. (2023) J Biol Chem "N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase." (0)

  • Overview

    PMID:
    36813232
    DOI:
    10.1016/j.jbc.2023.103053
    Status:
    Publication type:
    Journal_article
    WormBase ID:
    WBPaper00065036

    Paschinger K, Woels F, Yan S, Jin C, Vanbeselaere J, Dutkiewicz Z, Arcalis E, Malzl D, & Wilson IH (2023). N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase. J Biol Chem, 103053. doi:10.1016/j.jbc.2023.103053

    Simple organisms are often considered to have simple glycomes, but plentiful pauci- and oligomannosidic glycans overshadow the less abundant N-glycans with highly variable core and antennal modifications; Caenorhabditis elegans is no exception. By use of optimised fractionation and assessing wild-type in comparison to mutant strains lacking either the HEX-4 or HEX-5 β-N-acetylgalactosaminidases, we conclude that the model nematode has a total N-glycomic potential of 300 verified isomers. Three pools of glycans were analysed for each strain: either PNGase F-released and eluted from a reversed phase C18 resin with either water or 15% methanol or PNGase Ar-released. While the water-eluted fractions were dominated by typical pauci- and oligomannosidic glycans and the PNGase Ar-released pools by glycans with various core modifications, we found the methanol-eluted fractions contained a huge range of phosphorylcholine-modified structures with up to three antennae, sometimes with four N-acetylhexosamine residues in series. There were no major differences between the C. elegans wild-type and hex-5 mutant strains, but the hex-4 mutant strains displayed altered sets of methanol-eluted and PNGase Ar-released pools. In keeping with the specificity of HEX-4, there were more glycans capped with N-acetylgalactosamine in the hex-4 mutants, as compared to isomeric chito-oligomer motifs in the wild-type. Additionally, considering that fluorescence microscopy shows that a HEX-4::eGFP fusion protein co-localises with a Golgi tracker, we conclude that HEX-4 plays a significant role in late-stage Golgi processing of N-glycans in Caenorhabditis elegans. Furthermore, finding more 'parasite-like' structures in the model worm may facilitate the discovery of glycan-processing enzymes occurring in other nematodes.

    Authors: Paschinger K, Woels F, Yan S, Jin C, Vanbeselaere J, Dutkiewicz Z, Arcalis E, Malzl D, Wilson IH

    We thank Iain Wilson for curating this paper through ACKnowledge (Author Curation to Knowledgebase) 👍

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