<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Hewitson JP</submitter><funding>Asthma UK</funding><funding>American Asthma Foundation</funding><funding>National Institutes of Health</funding><funding>Wellcome Trust</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>157-170</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4776704</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>46(3)</volume><pubmed_abstract>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 N- and O-linked glycans released from Heligmosomoides polygyrus excretory-secretory products 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 tw</pubmed_abstract><journal>International journal for parasitology</journal><pubmed_title>Novel O-linked methylated glycan antigens decorate secreted immunodominant glycoproteins from the intestinal nematode Heligmosomoides polygyrus.</pubmed_title><pmcid>PMC4776704</pmcid><funding_grant_id>106122</funding_grant_id><funding_grant_id>106122/A/14/Z</funding_grant_id><funding_grant_id>GM62116</funding_grant_id><funding_grant_id>090281</funding_grant_id><funding_grant_id>U54 GM062116</funding_grant_id><funding_grant_id>P41 GM103694</funding_grant_id><funding_grant_id>SPD-2012-172</funding_grant_id><funding_grant_id>P41GM103694</funding_grant_id><funding_grant_id>10-0234</funding_grant_id><pubmed_authors>van Diepen A</pubmed_authors><pubmed_authors>Smit CH</pubmed_authors><pubmed_authors>Hokke CH</pubmed_authors><pubmed_authors>Koeleman CA</pubmed_authors><pubmed_authors>McSorley HJ</pubmed_authors><pubmed_authors>Nguyen DL</pubmed_authors><pubmed_authors>Murray J</pubmed_authors><pubmed_authors>Hewitson JP</pubmed_authors><pubmed_authors>Maizels RM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Novel O-linked methylated glycan antigens decorate secreted immunodominant glycoproteins from the intestinal nematode Heligmosomoides polygyrus.</name><description>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 N- and O-linked glycans released from Heligmosomoides polygyrus excretory-secretory products 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 tw</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Mar</publication><modification>2025-04-26T09:18:16.606Z</modification><creation>2019-03-27T02:10:25Z</creation></dates><accession>S-EPMC4776704</accession><cross_references><pubmed>26688390</pubmed><doi>10.1016/j.ijpara.2015.10.004</doi></cross_references></HashMap>