Studies on Galalpha3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin.
Studies on Galalpha3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin.
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Galalpha3 结合蛋白的研究：Marasmius oreades 凝集素和 Euonymus europaeus 凝集素的鞘糖脂结合特异性的比较。
DOI：
10.1093/glycob/cwg049
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发表时间：
2003
期刊：
影响因子：
4.3
通讯作者：
I. Goldstein
中科院分区：
文献类型：
--
作者：
S. Teneberg;Björn Alsén;J. Ångström;H. C. Winter;I. Goldstein
通过在薄层色谱图和微量滴定威尔斯孔中与鞘糖脂结合来检查来自小皮伞和欧洲小皮伞的Galalpha 3 Galbeta 4 GlcNAc结合凝集素的碳水化合物结合偏好。分枝Oreades凝集素结合到Galalpha 3-终止的鞘糖脂，优先选择2型链。B6 2型鞘糖脂（Galalpha 3 [Fucalpha 2] Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1Cer）优于B5鞘糖脂（Galalpha 3Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1Cer），表明α 2连接的Fuc被容纳在碳水化合物结合位点，提供了额外的相互作用。来自E. Europaeus具有更广泛的结合特异性。B6 2型鞘糖脂也是该凝集素的最佳配体，但也获得了与B6 1型鞘糖脂（Galalpha 3 [Fucalpha 2] Galbeta 3GlcNAcbeta 3Galbeta 4Glcbeta 1Cer）的结合。此外，H5 2型鞘糖脂（Fucalpha 2Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1Cer），缺乏末端α 3-连接的Gal，优于B5鞘糖脂，证明α 2-连接的Fuc对结合亲和力的显著贡献。E.这种凝集素也能与M. europaeus结合，而与M. oreades lectin，与x2鞘糖脂（GalNAcbeta 3Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1Cer）和GlcNAcbeta 3Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1Cer。A6 2型鞘糖脂（GalNAcalpha 3 [Fucalpha 2] Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1Cer）和GalNAcalpha 3Galbeta 4GlcNAcbeta 3Galbeta 4Glcbeta 1-Cer不被凝集素识别，尽管与B6 2型鞘糖脂和B5鞘糖脂相互作用。这些观察结果可以用Galalpha 3的2-位上的游离羟基的绝对要求和E.通过改变末端糖的方向，欧罗巴凝集素可以在靠近该位置处容纳GlcNAc乙酰氨基部分，而M.山毛榉凝集素不能。
The carbohydrate binding preferences of the Galalpha3Galbeta4 GlcNAc-binding lectins from Marasmius oreades and Euonymus europaeus were examined by binding to glycosphingolipids on thin-layer chromatograms and in microtiter wells. The M. oreades lectin bound to Galalpha3-terminated glycosphingolipids with a preference for type 2 chains. The B6 type 2 glycosphingolipid (Galalpha3[Fucalpha2]Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer) was preferred over the B5 glycosphingolipid (Galalpha3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer), suggesting that the alpha2-linked Fuc is accommodated in the carbohydrate binding site, providing additional interactions. The lectin from E. europaeus had broader binding specificity. The B6 type 2 glycosphingolipid was the best ligand also for this lectin, but binding to the B6 type 1 glycosphingolipid (Galalpha3[Fucalpha2]Galbeta3GlcNAcbeta3Galbeta4Glcbeta1Cer) was also obtained. Furthermore, the H5 type 2 glycosphingolipid (Fucalpha2Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer), devoid of a terminal alpha3-linked Gal, was preferred over the the B5 glycosphingolipid, demonstrating a significant contribution to the binding affinity by the alpha2-linked Fuc. The more tolerant nature of the lectin from E. europaeus was also demonstrated by the binding of this lectin, but not the M. oreades lectin, to the x2 glycosphingolipid (GalNAcbeta3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer) and GlcNAcbeta3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer. The A6 type 2 glycosphingolipid (GalNAcalpha3[Fucalpha2]Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer) and GalNAcalpha3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1-Cer were not recognized by the lectins despite the interaction with B6 type 2 glycosphingolipid and the B5 glycosphingolipid. These observations are explained by the absolute requirement of a free hydroxyl in the 2-position of Galalpha3 and that the E. europaea lectin can accommodate a GlcNAc acetamido moiety close to this position by reorienting the terminal sugar, whereas the M. oreades lectin cannot.
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影响因子：
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DOI：
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DOI：
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影响因子：
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