Glyco-DIA: a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Glyco-DIA : a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries. / Ye, Zilu; Mao, Yang; Clausen, Henrik; Vakhrushev, Sergey Y.
In: Nature Methods, Vol. 16, No. 9, 2019, p. 902-910.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Glyco-DIA
T2 - a method for quantitative O-glycoproteomics with in silico-boosted glycopeptide libraries
AU - Ye, Zilu
AU - Mao, Yang
AU - Clausen, Henrik
AU - Vakhrushev, Sergey Y
PY - 2019
Y1 - 2019
N2 - 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 core1 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 core1 O-glycans from 159 glycoproteins in a SingleShot analysis.
AB - 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 core1 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 core1 O-glycans from 159 glycoproteins in a SingleShot analysis.
U2 - 10.1038/s41592-019-0504-x
DO - 10.1038/s41592-019-0504-x
M3 - Journal article
C2 - 31384044
VL - 16
SP - 902
EP - 910
JO - Nature Methods
JF - Nature Methods
SN - 1548-7091
IS - 9
ER -
ID: 228734179