Glycoproteomic Analysis of Antibodies

• Published in: Molecular & cellular proteomics Vol. 12; no. 4; pp. 856 - 865
• Main Authors: Zauner, Gerhild, Selman, Maurice H.J., Bondt, Albert, Rombouts, Yoann, Blank, Dennis, Deelder, André M., Wuhrer, Manfred
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.04.2013; The American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; Antibodies - chemistry; Antibodies - metabolism; Carbohydrate Conformation; Carbohydrate Sequence; Glycoproteins - chemistry; Glycoproteins - metabolism; Glycosylation; Humans; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Peptide Fragments - chemistry; Protein Processing, Post-Translational; Proteomics; Review
• ISSN: 1535-9476; 1535-9484
• DOI: 10.1074/mcp.R112.026005

Antibody glycosylation has been shown to change with various processes. This review presents mass spectrometric approaches for antibody glycosylation analysis at the level of released glycans, glycopeptides, and intact protein. With regard to IgG fragment crystallizable glycosylation, mass spectrometry has shown its potential for subclass-specific, high-throughput analysis. In contrast, because of the vast heterogeneity of peptide moieties, fragment antigen binding glycosylation analysis of polyclonal IgG relies entirely on glycan release. Next to IgG, IgA has gained some attention, and studies of its O- and N-glycosylation have revealed disease-associated glycosylation changes. Glycoproteomic analyses of IgM and IgE are lagging behind but should complete our picture of glycosylation's influence on antibody function.