Analytical and Functional Aspects of Antibody Sialylation

MATERIALS AND METHODS: This review focuses on the role of antibody sialylation and methods for its quantitation. The recent attribution of the anti-inflammatory activity of IgG to the sialylation of its glycans in the Fc region has raised interest in the fine structure and analysis of the glycans. T...

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Autores principales: Stadlmann, Johannes, Pabst, Martin, Altmann, Friedrich
Formato: Texto
Lenguaje:English
Publicado: Springer US 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883086/
https://www.ncbi.nlm.nih.gov/pubmed/20390325
http://dx.doi.org/10.1007/s10875-010-9409-2
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author Stadlmann, Johannes
Pabst, Martin
Altmann, Friedrich
author_facet Stadlmann, Johannes
Pabst, Martin
Altmann, Friedrich
author_sort Stadlmann, Johannes
collection PubMed
description MATERIALS AND METHODS: This review focuses on the role of antibody sialylation and methods for its quantitation. The recent attribution of the anti-inflammatory activity of IgG to the sialylation of its glycans in the Fc region has raised interest in the fine structure and analysis of the glycans. The anti-inflammatory fraction of intravenous IgG could be isolated with the Sambucus nigra lectin. Experimental strategies for the assessment of antibody sialylation are discussed. RESULTS: Thorough analysis of the lectin-binding fraction revealed that the antibody Fc region only binds to S. nigra lectin when two sialic acids are present, whereas for other glycoprotein ligands, one sialic acid appears sufficient.
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spelling pubmed-28830862010-06-21 Analytical and Functional Aspects of Antibody Sialylation Stadlmann, Johannes Pabst, Martin Altmann, Friedrich J Clin Immunol Article MATERIALS AND METHODS: This review focuses on the role of antibody sialylation and methods for its quantitation. The recent attribution of the anti-inflammatory activity of IgG to the sialylation of its glycans in the Fc region has raised interest in the fine structure and analysis of the glycans. The anti-inflammatory fraction of intravenous IgG could be isolated with the Sambucus nigra lectin. Experimental strategies for the assessment of antibody sialylation are discussed. RESULTS: Thorough analysis of the lectin-binding fraction revealed that the antibody Fc region only binds to S. nigra lectin when two sialic acids are present, whereas for other glycoprotein ligands, one sialic acid appears sufficient. Springer US 2010-04-14 2010 /pmc/articles/PMC2883086/ /pubmed/20390325 http://dx.doi.org/10.1007/s10875-010-9409-2 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Stadlmann, Johannes
Pabst, Martin
Altmann, Friedrich
Analytical and Functional Aspects of Antibody Sialylation
title Analytical and Functional Aspects of Antibody Sialylation
title_full Analytical and Functional Aspects of Antibody Sialylation
title_fullStr Analytical and Functional Aspects of Antibody Sialylation
title_full_unstemmed Analytical and Functional Aspects of Antibody Sialylation
title_short Analytical and Functional Aspects of Antibody Sialylation
title_sort analytical and functional aspects of antibody sialylation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883086/
https://www.ncbi.nlm.nih.gov/pubmed/20390325
http://dx.doi.org/10.1007/s10875-010-9409-2
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AT pabstmartin analyticalandfunctionalaspectsofantibodysialylation
AT altmannfriedrich analyticalandfunctionalaspectsofantibodysialylation

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