Glyco-immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, College of Medicine, Chang-Gung University, Kwei-san, Tao-yuan 333, Taiwan.
FEBS Lett. 2010 Aug 20;584(16):3561-6. doi: 10.1016/j.febslet.2010.07.021. Epub 2010 Jul 17.
For the GalNAcalpha1--> specific Agaricus bisporus agglutinin (ABA) from an edible mushroom, the mechanism of polyvalent Galbeta1-->3/4GlcNAcbeta1--> complex in ABA-carbohydrate recognition has not been well defined since Gal and GlcNAc are weak ligands. By enzyme-linked lectinosorbent and inhibition assays, we show that the polyvalent Galbeta1-->3/4GlcNAcbeta1--> in natural glycans also play vital roles in binding and we propose that four different intensities of glycotopes (Galbeta1-3GalNAcalpha1-, GalNAcalpha1-Ser/Thr and Galbeta1-3/4GlcNAcbeta1-) construct three recognition systems at the same domain. This peculiar concept provides the most comprehensive mechanism for the attachment of ABA to target glycans and malignant cells at the molecular level.
对于一种来自可食用蘑菇的 GalNAcalpha1--特异性 Agaricus bisporus 凝集素（ABA），由于 Gal 和 GlcNAc 是弱配体，因此 ABA 中碳水化合物的多价 Galbeta1--3/4GlcNAcbeta1--复合物的识别机制尚未得到很好的定义。通过酶联凝集素吸附和抑制试验，我们表明天然聚糖中的多价 Galbeta1--3/4GlcNAcbeta1--也在结合中起重要作用，我们提出四个不同强度的糖基表位（Galbeta1-3GalNAcalpha1-、GalNAcalpha1-Ser/Thr 和 Galbeta1-3/4GlcNAcbeta1-）在同一结构域构建了三个识别系统。这种特殊的概念为 ABA 与靶聚糖和恶性细胞在分子水平上的附着提供了最全面的机制。
