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Volume 272, Number 27, Issue of July 4, 1997 pp. 16889-16895
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Binding Specificities of the Sialoadhesin Family of I-type Lectins
SIALIC ACID LINKAGE AND SUBSTRUCTURE REQUIREMENTS FOR BINDING OF MYELIN-ASSOCIATED GLYCOPROTEIN, SCHWANN CELL MYELIN PROTEIN, AND SIALOADHESIN

(Received for publication, February 19, 1997, and in revised form, April 9, 1997)

Brian E. Collins , Makoto Kiso ^¶ , Akira Hasegawa ^¶ , Michael B. Tropak , John C. Roder , Paul R. Crocker ^** and Ronald L. Schnaar

From the  Departments of Pharmacology and Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, the ^¶ Department of Applied Bioorganic Chemistry, Gifu University, Gifu 501-11, Japan, the  Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto M5G 1X5, Canada, and the ^** Imperial Cancer Research Fund Laboratories, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom

The carbohydrate binding specificities of three sialoadhesins, a subgroup of I-type lectins (immunoglobulin superfamily lectins), were compared by measuring lectin-transfected COS cell adhesion to natural and synthetic gangliosides. The neural sialoadhesins, myelin-associated glycoprotein (MAG) and Schwann cell myelin protein (SMP), had similar and stringent binding specificities. Each required an 2,3-linked sialic acid on the terminal galactose of a neutral saccharide core, and they shared the following rank-order potency of binding: G_Q1b  G_D1a = G_T1b  G_M3 = G_M4  G_M1, G_D1b, G_D3, G_Q1b (nonbinders). In contrast, sialoadhesin had less exacting specificity, binding to gangliosides that bear either terminal 2,3- or 2,8-linked sialic acids with the following rank-order potency of binding: G_Q1b > G_D1a = G_D1b = G_T1b = G_M3 = G_M4 > G_D3 = G_Q1b  G_M1 (nonbinder). CD22 did not bind to any ganglioside tested. Binding of MAG, SMP, and sialoadhesin was abrogated by chemical modification of either the sialic acid carboxylic acid group or glycerol side chain on a target ganglioside. Synthetic ganglioside G_M3 derivatives further distinguished lectin binding specificities. Deoxy and/or methoxy derivatives of the 4-, 7-, 8-, or 9-position of sialic acid attenuated or eliminated binding of MAG, as did replacement of the sialic acid acetamido group with a hydroxyl. In contrast, the 4- and 7-deoxysialic acid derivatives supported sialoadhesin binding at near control levels (the other derivatives did not support binding). These data are consistent with sialoadhesin binding to one face of the sialic acid moiety, whereas MAG (and SMP) may have more complex binding sites or may bind sialic acids only in the context of more restricted oligosaccharide conformations.

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