Synthesis and binding analysis of unique AG2 pentasaccharide to human Siglec-2 using NMR techniques.
Siglec-2 is a mammalian sialic acid binding protein expressed on B-cell surfaces and is involved in the modulation of B-cell mediated immune response. We synthesized a unique starfish ganglioside, AG2 pentasaccharide Galfbeta(1-3)Galpalpha(1-4)Neu5Acalpha(2-3)Galpbeta(1-4)Glcp, and found that the synthetic pentasaccharide binds to human Siglec-2 by performing (1)H NMR experiments. Saturation transfer difference NMR experiments indicated that the C7-C9 side-chain and the acetamide moiety of the central sialic acid residue were located in the binding face of human Siglec-2. We determined the binding epitope of AG2 pentasaccharide to human Siglec-2, as the Galpalpha(1-4)Neu5Acalpha(2-3)Galp unit.
Hanashima
Shinya
S
Structural Glycobiology Team, RIKEN Advanced Science Institute, Hirosawa 2-1, Saitama 351-0198, Japan.
Sato
Ken-Ichi
K
Naito
Yuko
Y
Takematsu
Hiromu
H
Kozutsumi
Yasunori
Y
Ito
Yukishige
Y
Yamaguchi
Yoshiki
Y
D001665:Binding Sites; D000939:Epitopes; D005732:Gangliosides / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009844:Oligosaccharides / Q000737:chemistry*; D011485:Protein Binding; D051918:Sialic Acid Binding Ig-like Lectin 2 / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism
D000939:Epitopes; D005732:Gangliosides; D009844:Oligosaccharides; D051918:Sialic Acid Binding Ig-like Lectin 2