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For the parasite <jats:italic>Toxoplasma gondii<\/jats:italic>, <jats:italic>N<\/jats:italic>\u2010glycosylation of proteins is crucial for initial adhesion to host cells, parasite motility, and consequently, its ability to invade host cells. However, the glycoproteome of <jats:italic>T. gondii<\/jats:italic> remains largely unknown. In this study, we used the \u03b1\u2010mannose\u2010specific <jats:italic>Burkholderia cenocepacia<\/jats:italic> lectin A (BC2L\u2010A) to enrich glycopeptides from <jats:italic>T. gondii<\/jats:italic> tachyzoites and analysed them by tandem mass spectrometry. The data enable the identification of over 100 <jats:italic>N<\/jats:italic>\u2010glycoproteins with the glycosylation site(s) and the composition of the <jats:italic>N<\/jats:italic>\u2010glycans at each site. <jats:italic>T. gondii<\/jats:italic> glycoproteins include known virulence factors, vaccine candidates as well as numerous uncharacterised proteins. These data provide ground knowledge to deepen our understanding of the role of glycoproteins in invasion and assist the rational design of vaccines.<\/jats:p>","DOI":"10.1002\/pmic.202400239","type":"journal-article","created":{"date-parts":[[2025,3,12]],"date-time":"2025-03-12T10:18:51Z","timestamp":1741774731000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["<i>N<\/i>\u2010Glycoproteomics of the Apicomplexan Parasite <i>Toxoplasma gondii<\/i>"],"prefix":"10.1002","volume":"25","author":[{"given":"Vanessa","family":"Horn","sequence":"first","affiliation":[{"name":"Department of Clinical Biochemistry OE4340 Hannover Medical School  Hannover Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patricia","family":"Zarnovican","sequence":"additional","affiliation":[{"name":"Department of Clinical Biochemistry OE4340 Hannover Medical School  Hannover 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