Glycoproteomic analysis of antibodies
Molecular and Cellular Proteomics , Volume 12 - Issue 4 p. 856- 865
Antibody glycosylation has been shown to change with various processes. This review presents mass spectro-metric approaches for antibody glycosylation analysis at the level of released glycans, glycopeptides, and intact protein. With regard to IgG fragment crystallizable glyco-sylation, 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 poly-clonal 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 and Cellular Proteomics|
|This work was funded by the European Commission 7th Framework Programme; grant id fp7/278535 - Methods for high-throughput (HTP) analysis of protein glycosylation (HIGHGLYCAN)|
|Organisation||Erasmus MC: University Medical Center Rotterdam|
Zauner, G, Selman, M.H.J, Bondt, A, Rombouts, Y, Blank, D, Deelder, A.M, & Wuhrer, M. (2013). Glycoproteomic analysis of antibodies. Molecular and Cellular Proteomics (Vol. 12, pp. 856–865). doi:10.1074/mcp.R112.026005