Takeuchi Tomoharu, Sennari Remi, Sugiura Ken-ichi, Tateno Hiroaki, Hirabayashi Jun, Kasai Ken-ichi
Department of Biological Chemistry, School of Pharmaceutical Sciences, Teikyo University, Sagamihara, Kanagawa, Japan.
Biochem Biophys Res Commun. 2008 Dec 5;377(1):303-6. doi: 10.1016/j.bbrc.2008.10.001. Epub 2008 Oct 9.
C-type lectins are a family of proteins with an affinity to carbohydrates in the presence of Ca(2+). 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 on evanescent-field excited fluorescence. CLEC-79 exhibited affinity to sugars containing galactose at the non-reducing terminal, especially to the Galbeta1-3GalNAc structure, in the presence of Ca(2+). Combined with structural information of the glycans of C. elegans, these results suggest that CLEC-79 preferentially binds to O-glycans in vivo.
C型凝集素是一类在钙离子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,已确定了近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,它们的产物均未显示出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。通过使用基于倏逝场激发荧光新开发的糖缀合物微阵列,发现其中一个由clec-79编码的蛋白具有糖结合活性。在钙离子存在下,CLEC-79对非还原末端含有半乳糖的糖类表现出亲和力,尤其对Galβ1-3GalNAc结构。结合秀丽隐杆线虫聚糖的结构信息,这些结果表明CLEC-79在体内优先结合O-聚糖。