Synthesis and binding analysis of unique AG2 pentasaccharide to human Siglec-2 using NMR techniques

Bioorg Med Chem. 2010 Jun 1;18(11):3720-5. doi: 10.1016/j.bmc.2010.03.062. Epub 2010 Mar 30.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Epitopes
  • Gangliosides / chemistry
  • Humans
  • Magnetic Resonance Spectroscopy / methods*
  • Oligosaccharides / chemistry*
  • Protein Binding
  • Sialic Acid Binding Ig-like Lectin 2 / chemistry*
  • Sialic Acid Binding Ig-like Lectin 2 / immunology
  • Sialic Acid Binding Ig-like Lectin 2 / metabolism

Substances

  • Epitopes
  • Gangliosides
  • Oligosaccharides
  • Sialic Acid Binding Ig-like Lectin 2