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A more recent version of this article appeared on August 15, 2003
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Papers In Press, published online ahead of print May 28, 2003
J. Biol. Chem, 10.1074/jbc.M304331200
Submitted on April 25, 2003
Revised on May 27, 2003
Accepted on May 28, 2003

Sialoside specificity of the Siglec family assessed using novel multivalent probes: Identification of potent inhibitors of myelin associated glycoproteinz

Ola Blixt, Brian E. Collins, Ingrid M. van den Nieuwenhof, Paul R. Crocker, and James C. Paulson

Molecular Biology & Molecular Experimental Medicines, The Scripps Research Institute, San Diego, CA 92037

Corresponding Author: jpaulson{at}scripps.edu

Ten of the eleven known human siglecs or their murine orthologs have been evaluated for their specificity for over twenty-five 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 (SAAP) conjugate. Each siglec was found to have a unique specificity for binding sixteen different sialoside-SAA P 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 penult i mate 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-lin k ed T-antigen (Galbeta (1-3)GalNAcalpha OThr) as compared to alpha -methyl-NeuAc .2o


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