Binding Affinities of NKG2D and CD94 to Sialyl Lewis X-Expressing <i>N</i>-Glycans and Heparin

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  • Higai Koji
    Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
  • Suzuki Chiho
    Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
  • Imaizumi Yuzo
    Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
  • Xin Xin
    Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
  • Azuma Yutaro
    Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
  • Matsumoto Kojiro
    Department of Clinical Chemistry, Faculty of Pharmaceutical Sciences, Toho University

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  • Binding affinities of NKG2D and CD94 to sialyl Lewis X-expressing N-glycans and heparin

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Abstract

Lectin-like receptors natural killer group 2D (NKG2D) and CD94 on natural killer (NK) cells bind to α2,3-NeuAc-containing N-glycans and heparin/heparan sulfate (HS). Using recombinant glutathione S-transferase-fused extracellular lectin-like domains of NKG2D (rGST-NKG2Dlec) and CD94 (rGST-CD94lec), we evaluated their binding affinities (Kd) to high sialyl Lewis X (sLeX)-expressing transferrin secreted by HepG2 cells (HepTf) and heparin-conjugated bovine serum albumin (Heparin-BSA), using quartz crystal microbalance (QCM) and enzyme immunoassay (EIA) microplate methods. Kd values obtained by linear reciprocal plots revealed good coincidence between the two methods. Kd values of rGST-NKG2Dlec obtained by QCM and EIA, respectively, were 1.19 and 1.11 μM for heparin-BSA >0.30 and 0.20 μM for HepTf, while those of rGST-CD94lec were 1.31 and 1.45 μM for HepTf >0.37 and 0.36 μM for heparin-BSA. These results suggested that these glycans can interact with NKG2D and CD94 to modulate NK cell-dependent cytotoxicity.

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