NKG2D: Binding Properties for Glycan Ligands, and Mutagenesis Analysis
| Autor: | Kazuyuki Yanai, Megumi Kimura, Koji Higai, Yuzo Imaizumi, Yutaro Azuma, Kojiro Matsumoto, Sayo Matsumoto |
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| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Glycan biology Biomedical Engineering Biophysics hemic and immune systems chemical and pharmacologic phenomena Bioengineering Biochemistry Molecular biology carbohydrates (lipids) chemistry.chemical_compound Sulfation Sialyl-Lewis X chemistry Transferrin MHC class I biology.protein Binding site Bovine serum albumin Receptor Biotechnology |
| Zdroj: | The Open Biotechnology Journal. 5:33-38 |
| ISSN: | 1874-0707 |
| DOI: | 10.2174/1874070701105010033 |
| Popis: | Killer lectin-like receptor NKG2D, which is found on natural killer cells, recognizes MHC class 1-related ligands and also interacts with glycan ligands, heparin-conjugated bovine serum albumin (heparin-BSA) and sialyl Lewis X (sLeX) on multi-antennary N-glycans on transferrin secreted by HepG2 cells (HepTF). Using the glutathione-Stransferase- fused extracellular domain (AA 73-216) of NKG2D (rGST-NKG2D) and seven site-directed mutants, we explored in detail the binding of NKG2D to sulfate-containing glycan-BSA and HepTF. rGST-NKG2D binds to sulfatecontaining glycan-BSA with Kd values of 25 nM ±15 for λ-carrageenan-BSA, 66 ±23 nM for fucoidan-BSA, and 1.5±0.5 μM for heparan sulfate-BSA. Of the site-directed rGST-NKG2D mutants, Y152A, Q185A, K197A, Y199A, E201A, and N207A reduced binding to these glycans. These results indicate that NKG2D interacts with highly sulfated- and α2,3- NeuAc-containing glycans and suggest that the glycan-binding sites on NKG2D are shared between sulfate- and α2,3- NeuAc-containing glycans, and might overlap with protein ligand binding sites. |
| Databáze: | OpenAIRE |
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