A C-type lectin of Caenorhabditis elegans: Its sugar-binding property revealed by glycoconjugate microarray analysis
A C-type lectin of Caenorhabditis elegans: Its sugar-binding property revealed by glycoconjugate microarray analysis
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DOI：
10.1016/j.bbrc.2008.10.001
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发表时间：
2008-12-05
影响因子：
3.1
通讯作者：
Kasai, Ken-ichi
中科院分区：
文献类型：
--
作者：
Takeuchi, Tomoharu;Sennari, Remi;Kasai, Ken-ichi
C 型凝集素是在 Ca2+ 存在下对碳水化合物具有亲和力的蛋白质家族。在秀丽隐杆线虫的基因组中，已分配了近 300 个编码含有 C 型凝集素样结构域 (CTLD) 的蛋白质的基因。然而，他们的产品都没有被证明具有碳水化合物结合活性。在本研究中，我们选择了6个潜在的C型凝集素基因并制备了相应的重组蛋白。其中一种由 clec-79 编码的化合物通过使用新开发的基于糖复合物微阵列的油倏逝场激发荧光被发现具有糖结合活性。 CLEC-79 在 Ca2+ 存在下表现出对非还原端含有半乳糖的糖的亲和力，特别是对 Gal beta 1-3GalNAc 结构的亲和力。结合线虫聚糖的结构信息，这些结果表明 CLEC-79 在体内优先与 O-聚糖结合。 (C) 2008 Elsevier Inc. 保留所有权利。
C-type lectins are a family of proteins with an affinity to carbohydrates in the presence of Ca2+. In the genome of Caenorhabditis elegans, almost 300 genes encoding proteins containing C-type lectin-like domains (CTLDs) have been assigned. However, none of their products has ever been shown to have carbohydrate-binding activity In the present study, we selected 6 potential C-type lectin genes and prepared corresponding recombinant proteins. One of them encoded by clec-79 Was found to have sugar-binding activity by using a newly developed glycoconjugate microarray based oil evanescent-field excited fluorescence.. CLEC-79 exhibited affinity to Sugars containing galactose at the non-reducing terminal, especially to the Gal beta 1-3GalNAc structure, in the presence of Ca2+. Combined with structural information of the glycans of C. elegans, these results suggest that CLEC-79 preferentially binds to O-glycans in vivo. (C) 2008 Elsevier Inc. All rights reserved.