Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Sialoside specificity of the siglec family assessed using novel multivalent probes - identification of potent inhibitors of myelin-associated glycoprotein

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Blixt, O.
  • Collins, B. E.
  • van den Nieuwenhof, I. M.
  • Crocker, P. R.
  • Paulson, James

publication date

  • August 2003

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Ten of the 11 known human siglecs or their murine orthologs have been evaluated for their specificity for over 25 synthetic sialosides representing most of the major sequences terminating carbohydrate groups of glycoproteins and glycolipids. Analysis has been performed using a novel multivalent platform comprising biotinylated sialosides bound to a streptavidin-alkaline phosphatase conjugate. Each siglec was found to have a unique specificity for binding 16 different sialoside-streptavidin-alkaline phosphatase probes. The relative affinities of monovalent sialosides were assessed for each siglec in competitive inhibition studies. The quantitative data obtained allows a detailed analysis of each siglec for the relative importance of sialic acid and the penultimate oligosaccharide sequence on binding affinity and specificity. Most remarkable was the finding that myelin-associated glycoprotein (Siglec-4) binds with 500-10,000-fold higher affinity to a series of mono- and di-sialylated derivatives of the O-linked T-antigen (Galbeta(1-3)-GalNAc(alpha)OThr) as compared with alpha-methyl-NeuAc.

subject areas

  • Alkaline Phosphatase
  • Animals
  • Antigens, CD
  • Antigens, Differentiation, B-Lymphocyte
  • Antigens, Differentiation, Myelomonocytic
  • CHO Cells
  • Carbohydrate Sequence
  • Cell Adhesion Molecules
  • Chimera
  • Cricetinae
  • Enzyme-Linked Immunosorbent Assay
  • Galactosides
  • Glycolipids
  • Glycoproteins
  • Humans
  • Lectins
  • Membrane Glycoproteins
  • Mice
  • Molecular Sequence Data
  • N-Acetylneuraminic Acid
  • Protein Binding
  • Receptors, Immunologic
  • Sialic Acid Binding Ig-like Lectin 1
  • Sialic Acid Binding Ig-like Lectin 2
  • Sialic Acid Binding Immunoglobulin-like Lectins
  • Streptavidin
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M304331200

PubMed ID

  • 12773526
scroll to property group menus

Additional Document Info

start page

  • 31007

end page

  • 31019

volume

  • 278

issue

  • 33

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support