title: Glycoproteomic analysis of antibodies.
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.
authors: Biomolecular Mass Spectrometry Unit, Postbus 9600, 2300RC Leiden University Medical Center, Leiden, The Netherlands.
authors: Gerhild
authors: G
authors: Zauner
authors: Maurice H J
authors: MH
authors: Selman
authors: Albert
authors: A
authors: Bondt
authors: Yoann
authors: Y
authors: Rombouts
authors: Dennis
authors: D
authors: Blank
authors: André M
authors: AM
authors: Deelder
authors: Manfred
authors: M
authors: Wuhrer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000378:metabolism*; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D040901:Proteomics
chemical_list: D000906:Antibodies; D006023:Glycoproteins; D010446:Peptide Fragments