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Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes

Open access
Blixt, Ola, Collins, Brian E., van den Nieuwenhof, Ingrid M., Crocker, Paul R., Paulson, James C.·2003·Journal of Biological Chemistry

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.

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Metadata

Authors
Blixt, O., Collins, B. E., van den Nieuwenhof, I. M., Crocker, P. R., & Paulson, J. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-08
Volume
278
Issue
33
Pages
31007-31019
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1975933816
Cited by
245
References
2
FWCI
4.72
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes. https://app.cochat.ai/papers/10.1074/jbc.m304331200
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Blixt, O., Collins, B. E., van den Nieuwenhof, I. M., Crocker, P. R., & Paulson, J. C. (2003). Sialoside Specificity of the Siglec Family Assessed Using Novel Multivalent Probes. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m304331200

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