Analytical and functional aspects of antibody sialylation

Johannes Stadlmann, Martin Pabst, Friedrich Altmann*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

52 Citations (Scopus)


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 antiinflammatory 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.

Original languageEnglish
Pages (from-to)S15-S19
JournalJournal of Clinical Immunology
Issue numberSUPPL. 1
Publication statusPublished - 1 May 2010


  • Anti-inflammatory
  • Antibody glycosylation
  • IVIG
  • Sialic acid


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