Lectin structure-activity: The story is never over
Lectin structure-activity: The story is never over
复制标题
DOI：
10.1021/jf0201879
复制
发表时间：
2002-10-23
影响因子：
6.1
通讯作者：
Goldstein, IJ
中科院分区：
文献类型：
--
作者：
Goldstein, IJ
在过去的十年中，植物凝集素生物化学的进展取得了长足的进步。生物物理技术和分子生物学的技术进步、合成寡糖的可用性以及具有独特碳水化合物结合特性的凝集素的表征是这些进步的原因。该实验室的研究支持了尚未做出有趣的新发现的观点。最近从真菌（多孔鳞状）中分离出一种新的凝集素，它以高亲和力识别 Neu5Ac α2,6 Gal beta1,4 GlcNAc/Glc 三糖表位。凝集素不会与绵羊颌下粘蛋白中的 alpha2,3 连接的 Neu5Ac 或 Neu5Ac alpha2,6 GalNAc 基团相互作用。 Xanthosoma sagittifolium (L) 的块茎中存在一种不寻常的凝集素，具有两个明显不同的碳水化合物结合位点。一种位点识别低聚甘露糖残基簇。另一种类型的结合位点最适合在其三个非还原末端具有 LacNAc 或乳-N-二糖（Gal 1,beta1, 3GlcNAc）基团的非唾液酸化三触角寡糖。香蕉凝集素也已被研究。它可识别 α 和 β1,3-连接的葡糖基寡糖，利用支链三糖 Man α1,6[Man α1,3]Man 生成沉淀素曲线，并与含有 β1,6-葡糖基端基的 β-葡聚糖结合。
Advances in plant lectin biochemistry have made great strides during the past decade. Technical advances in biophysical techniques and molecular biology, the availability of synthetic oligosaccharides, and characterization of lectins with unique carbohydrate-binding properties are responsible for these advances. Studies in this laboratory support the view that interesting new discoveries are yet to be made. A new lectin was recently isolated from a fungus (Polyporous squamosus) that recognizes the Neu5Ac alpha2,6 Gal beta1,4 GlcNAc/Glc trisaccharide epitope with high affinity. The lectin does not interact with alpha2,3-linked Neu5Ac or Neu5Ac alpha2,6 GalNAc groups as occur in ovine submaxillary mucin. An unusual lectin with two distinctly different carbohydrate-binding sites is present in tubers of Xanthosoma sagittifolium (L). One species of sites recognizes clusters of oligomannosyl residues. The other type of binding site best accommodates a nonsialylated, triantennary oligosaccharide having LacNAc or Lacto-N-biose (Gal 1,beta1, 3GlcNAc) groups at its three nonreducing termini. The banana lectin has also been studied. It recognizes both alpha and beta1,3-linked glucosyl oligosaccharides, generates a precipitin curve with the branched trisaccharide Man alpha1,6[Man alpha1,3]Man, and binds to beta-glucans containing beta1,6-glucosyl end groups.