Stadlmann Johannes, Pabst Martin, Altmann Friedrich
Department of Chemistry, University of Natural Resources and Applied Life Sciences (BOKU), Muthgasse 18, 1190, Vienna, Austria.
J Clin Immunol. 2010 May;30 Suppl 1(Suppl 1):S15-9. doi: 10.1007/s10875-010-9409-2.
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.
本综述聚焦于抗体唾液酸化的作用及其定量方法。近期将IgG的抗炎活性归因于其Fc区域聚糖的唾液酸化，这引发了人们对聚糖精细结构及分析的兴趣。静脉注射IgG的抗炎部分可用黑接骨木凝集素分离。本文讨论了评估抗体唾液酸化的实验策略。
对凝集素结合部分的深入分析表明，只有当存在两个唾液酸时，抗体Fc区域才会与黑接骨木凝集素结合，而对于其他糖蛋白配体，一个唾液酸似乎就足够了。
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