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. 2017 May 31;8:608. doi: 10.3389/fimmu.2017.00608

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Copyright © 2017 de Haan, Reiding, Krištić, Hipgrave Ederveen, Lauc and Wuhrer.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Glycoforms detected by the three synergetic analysis methods. Representative data and analytes detected in the analysis of the pooled CD-1 sample, showing (A) immunoglobulin G1 (IgG1) fragment crystallizable (Fc)-glycopeptides analyzed by nanoliquid chromatography mass spectrometry (nanoLC-MS), (B) the 20 most abundant released glycans of total IgG analyzed by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF)-MS after linkage-specific sialic acid derivatization, and (C) released glycans of total IgG analyzed by ultraperformance liquid chromatography (UPLC)-fluorescence after 2-AB labeling. Except for the sialic acid linkage in the MALDI-TOF-MS analysis (B), and the antenna galactosylation in the UPLC-fluorescence analysis (C), the monosaccharide linkages were not determined. The proposed glycan structures are based on fragmentation and literature (17, 23, 35, 36).