A C-type lectin of Caenorhabditis elegans: its sugar-binding property revealed by glycoconjugate microarray analysis |
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Authors: | Takeuchi Tomoharu Sennari Remi Sugiura Ken-ichi Tateno Hiroaki Hirabayashi Jun Kasai Ken-ichi |
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Institution: | a Department of Biological Chemistry, School of Pharmaceutical Sciences, Teikyo University, 1091-1 Suarashi, Sagamiko, Sagamihara, Kanagawa 229-0195, Japan b Lectin Application and Analysis Team, Research Center for Medical Glycoscience, AIST, Central 2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan |
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Abstract: | 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 on evanescent-field excited fluorescence. CLEC-79 exhibited affinity to sugars containing galactose at the non-reducing terminal, especially to the Galβ1-3GalNAc 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. |
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Keywords: | CRD carbohydrate recognition domain CTLD C-type lectin-like domain TBS Tris-buffered saline |
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