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

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 (K(d)) 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. K(d) values obtained by linear reciprocal plots revealed good coincidence between the two methods. K(d) 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.

journal_name

Biol Pharm Bull

authors

Higai K,Suzuki C,Imaizumi Y,Xin X,Azuma Y,Matsumoto K

doi

10.1248/bpb.34.8

subject

Has Abstract

pub_date

2011-01-01 00:00:00

pages

8-12

issue

1

eissn

0918-6158

issn

1347-5215

pii

JST.JSTAGE/bpb/34.8

journal_volume

34

pub_type

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