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Probing sialic acid binding Ig-like lectins (siglecs) with sulfated oligosaccharides

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Abstract

Soluble siglecs-1,-4,-5,-6,-7,-8,-9, and-10 were probed with polyacrylamide glycoconjugates in which: 1) the Neu5Ac residue was substituted by a sulfate group (Su); 2) glycoconjugates contained both Su and Neu5Ac; 3) sialoglycoconjugates contained a tyrosine-O-sulfate residue. It was shown that sulfate derivatives of LacNAc did not bind siglecs-1,-4,-5,-6,-7,-8,-9, and-10; binding of 6′-O-Su-LacNAc to siglec-8 was stronger than binding of 3′SiaLacNAc. The relative affinity of 3′-O-Su-TF binding to siglecs-1,-4, and-8 was similar to that of 3′SiaTF. 3′-O-Su-Lec displayed two-fold weaker binding to siglec-1 and siglec-4 than 3′SiaLec. The interaction of soluble siglecs with sulfated oligosaccharides containing sialic acid was also studied. It was shown that siglecs-1,-4,-5,-6,-7,-9, and-10 did not interact with these compounds; binding of 6-O-Su-3′SiaLacNAc and 6-O-Su-3′SiaTF to siglec-8 was weaker than that of the corresponding sulfate-free sialoside probes. Siglec-8 displayed affinity to 6′-O-Su-LacNAc and 6′-O-Su-SiaLex, and defucosylation of the latter compound led to an increase in the binding. Sialoside probes containing tyrosine-O-sulfate residue did not display increased affinity to siglecs-1 and-5 compared with glycoconjugates containing only sialoside. Cell-bound siglecs-1,-5,-7, and-9 did not interact with 6-O-Su-3′SiaLacNAc, whereas the sulfate-free probe 3′SiaLacNAc demonstrated binding. In contrast, the presence of sulfate in 6-O-Su-6′SiaLacNAc did not affect binding of the sialoside probe to siglecs. 6′-O-Su-SiaLex displayed affinity to cell-bound siglecs-1 and-5; its isomer 6-O-Su-SiaLex bound more strongly to siglecs-1,-5, and-9 than SiaLex.

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Abbreviations

BSA:

bovine serum albumin

CHO-siglec:

CHO cells transfected with siglec vector

fluo:

fluorescein

Glyc-PAA:

polyacrylamide glycoconjugate

PBA:

PBS containing 0.2% BSA

PBS:

phosphate buffered saline containing 0.01 M Na2HPO4, 0.01 M NaH2PO4, 0.15 M NaCl, pH 7.3

siglec-Fc:

chimeric protein containing full-sized extracellular region hSiglec and Fc region of human IgG

sTyr:

sulfotyrosine (tyrosine-O-sulfate)

TBS:

50 mM Tris-HCl buffer containing 150 mM NaCl, pH 7.5

TBA:

TBS containing 0.2% BSA

Versene solution:

PBS containing 0.02% EDTA

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Authors and Affiliations

  1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia

    E. M. Rapoport, G. V. Pazynina, M. A. Sablina & N. V. Bovin

  2. The Wellcome Trust Biocentre, School of Life Sciences, University of Dundee DD1 5EH, Scotland, UK

    P. R. Crocker

Authors
  1. E. M. Rapoport
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  2. G. V. Pazynina
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  3. M. A. Sablina
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  4. P. R. Crocker
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  5. N. V. Bovin
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Corresponding author

Correspondence to N. V. Bovin.

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Original Russian Text © E. M. Rapoport, G. V. Pazynina, M. A. Sablina, P. R. Crocker, N. V. Bovin, 2006, published in Biokhimiya, 2006, Vol. 71, No. 5, pp. 615–625.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM05-263, April 2, 2006.

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Rapoport, E.M., Pazynina, G.V., Sablina, M.A. et al. Probing sialic acid binding Ig-like lectins (siglecs) with sulfated oligosaccharides. Biochemistry (Moscow) 71, 496–504 (2006). https://doi.org/10.1134/S0006297906050051

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  • DOI: https://doi.org/10.1134/S0006297906050051

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