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Glycoproteomic Analysis of Antibodies
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 spectrome...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Biochemistry and Molecular Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3617332/ https://www.ncbi.nlm.nih.gov/pubmed/23325769 http://dx.doi.org/10.1074/mcp.R112.026005 |
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author | Zauner, Gerhild Selman, Maurice H. J. Bondt, Albert Rombouts, Yoann Blank, Dennis Deelder, André M. Wuhrer, Manfred |
author_facet | Zauner, Gerhild Selman, Maurice H. J. Bondt, Albert Rombouts, Yoann Blank, Dennis Deelder, André M. Wuhrer, Manfred |
author_sort | Zauner, Gerhild |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3617332 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-36173322013-05-29 Glycoproteomic Analysis of Antibodies Zauner, Gerhild Selman, Maurice H. J. Bondt, Albert Rombouts, Yoann Blank, Dennis Deelder, André M. Wuhrer, Manfred Mol Cell Proteomics Review 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. The American Society for Biochemistry and Molecular Biology 2013-04 2013-01-16 /pmc/articles/PMC3617332/ /pubmed/23325769 http://dx.doi.org/10.1074/mcp.R112.026005 Text en © 2013 by The American Society for Biochemistry and Molecular Biology, Inc. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Review Zauner, Gerhild Selman, Maurice H. J. Bondt, Albert Rombouts, Yoann Blank, Dennis Deelder, André M. Wuhrer, Manfred Glycoproteomic Analysis of Antibodies |
title | Glycoproteomic Analysis of Antibodies |
title_full | Glycoproteomic Analysis of Antibodies |
title_fullStr | Glycoproteomic Analysis of Antibodies |
title_full_unstemmed | Glycoproteomic Analysis of Antibodies |
title_short | Glycoproteomic Analysis of Antibodies |
title_sort | glycoproteomic analysis of antibodies |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3617332/ https://www.ncbi.nlm.nih.gov/pubmed/23325769 http://dx.doi.org/10.1074/mcp.R112.026005 |
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