Journal
JOURNAL OF CLINICAL IMMUNOLOGY
Volume 30, Issue -, Pages S15-S19Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10875-010-9409-2
Keywords
Antibody glycosylation; sialic acid; IVIG; anti-inflammatory
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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. 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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