Glycoproteomic Analysis of Antibodies

G Zauner, MHJ Selman, Albert Bondt, Y Rombouts, D Blank, AM Deelder, M Wuhrer

Research output: Contribution to journalArticleAcademicpeer-review

121 Citations (Scopus)

Abstract

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. Molecular & Cellular Proteomics 12: 10.1074/mcp.R112.026005, 856-865, 2013.
Original languageUndefined/Unknown
Pages (from-to)856-865
Number of pages10
JournalMolecular & Cellular Proteomics
Volume12
Issue number4
DOIs
Publication statusPublished - 2013

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