Oxonium ion scanning mass spectrometry for large-scale plasma glycoproteomics
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Matthew EH White Ludwig R Sinn D Marc Jones Joost de Folter Simran Aulakh Ziyue Wang Helen R Flynn Lynn Krüger Pinkus Tober-Lau Vadim Demichev Florian Kurth Michael Mülleder Véronique Blanchard Christoph Messner Markus RalserAbstract
Protein glycosylation, a complex and heterogeneous post-translational modification that is frequently dysregulated in disease, has been difficult to analyse at scale. Here we report a data-independent acquisition technique for the large-scale mass-spectrometric quantification of glycopeptides in plasma samples. The technique, which we named 'OxoScan-MS', identifies oxonium ions as glycopeptide fragments and exploits a sliding-quadrupole dimension to generate comprehensive and untargeted oxonium ion maps of precursor masses assigned to fragment ions from non-enriched plasma samples. By applying OxoScan-MS to quantify 1,002 glycopeptide features in the plasma glycoproteomes from patients with COVID-19 and healthy controls, we found that severe COVID-19 induces differential glycosylation in IgA, haptoglobin, transferrin and other disease-relevant plasma glycoproteins. OxoScan-MS may allow for the quantitative mapping of glycoproteomes at the scale of hundreds to thousands of samples.
Journal details
Journal
Nature Biomedical Engineering
Volume
8
Issue number
3
Pages
233-247
Available online
Publication date
Full text links
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10.1038/s41551-023-01067-5
Europe PubMed Central
37474612
Pubmed
37474612
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The publication was previously a preprint.
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