Article ; Online: Comparison of N-Glycopeptide to Released N-Glycan Abundances and the Influence of Glycopeptide Mass and Charge States on N-Linked Glycosylation of IgG Antibodies.
2024 Volume 23, Issue 4, Page(s) 1443–1457
Abstract: We report the comparison of mass-spectral-based abundances of tryptic glycopeptides to fluorescence abundances of released labeled glycans and the effects of mass and charge state and in-source fragmentation on glycopeptide abundances. The primary ... ...
Abstract | We report the comparison of mass-spectral-based abundances of tryptic glycopeptides to fluorescence abundances of released labeled glycans and the effects of mass and charge state and in-source fragmentation on glycopeptide abundances. The primary glycoforms derived from Rituximab, NISTmAb, Evolocumab, and Infliximab were high-mannose and biantennary complex galactosylated and fucosylated N-glycans. Except for Evolocumab, in-source ions derived from the loss of HexNAc or HexNAc-Hex sugars are prominent for other therapeutic IgGs. After excluding in-source fragmentation of glycopeptide ions from the results, a linear correlation was observed between fluorescently labeled N-glycan and glycopeptide abundances over a dynamic range of 500. Different charge states of human IgG-derived glycopeptides containing a wider variety of abundant attached glycans were also investigated to examine the effects of the charge state on ion abundances. These revealed a linear dependence of glycopeptide abundance on the mass of the glycan with higher charge states favoring higher-mass glycans. Findings indicate that the mass spectrometry-based bottom-up approach can provide results as accurate as those of glycan release studies while revealing the origin of each attached glycan. These site-specific relative abundances are conveniently displayed and compared using previously described glycopeptide abundance distribution spectra "GADS" representations. Mass spectrometry data are available from the MAssIVE repository (MSV000093562). |
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MeSH term(s) | Humans ; Glycosylation ; Immunoglobulin G ; Tandem Mass Spectrometry ; Glycopeptides/analysis ; Polysaccharides/chemistry ; Ions |
Chemical Substances | Immunoglobulin G ; Glycopeptides ; Polysaccharides ; Ions |
Language | English |
Publishing date | 2024-03-07 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 2078618-9 |
ISSN | 1535-3907 ; 1535-3893 |
ISSN (online) | 1535-3907 |
ISSN | 1535-3893 |
DOI | 10.1021/acs.jproteome.3c00904 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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