Journal
NATURE METHODS
Volume 16, Issue 9, Pages 902-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41592-019-0504-x
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Funding
- Lundbeck Foundation
- Mizutani Foundation
- Danish National Research Foundation [DNRF107]
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We report a liquid chromatography coupled to tandem mass spectrometry O-glycoproteomics strategy using data-independent acquisition (DIA) mode for direct analysis of O-glycoproteins. This approach enables characterization of glycopeptides and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries (though it does not allow for direct unambiguous glycosite identification). The method relies on a spectral library of O-glycopeptides; the Glyco-DIA library contains sublibraries obtained from human cell lines and human serum, and it currently covers 2,076 O-glycoproteins (11,452 unique glycopeptide sequences) and the 5 most common corel O-glycan structures. Applying the Glyco-DIA library to human serum without enrichment for glycopeptides enabled us to identify and quantify 269 distinct glycopeptide sequences bearing up to 5 different corel O-glycans from 159 glycoproteins in a SingleShot analysis.
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