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

Brian E. Collins, Makoto Kiso, Akira Hasegawa, Michael B. Tropak, John C. Roder, Paul R. Crocker, Ronald Lee Schnaar

Research output: Contribution to journalArticle

Abstract

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 α2,3-linked sialic acid on the terminal galactose of a neutral saccharide core, and they shared the following rank-order potency of binding: G(Q1bα) >> 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 α2,3- or α2,8-linked sialic acids with the following rank- order potency of binding: G(Q1bα) > 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 acetamide 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.

Original languageEnglish (US)
Pages (from-to)16889-16895
Number of pages7
JournalJournal of Biological Chemistry
Volume272
Issue number27
DOIs
StatePublished - Jul 4 1997

Fingerprint

Sialic Acid Binding Ig-like Lectin 1
Myelin-Associated Glycoprotein
Myelin Proteins
Schwann Cells
N-Acetylneuraminic Acid
Lectins
Gangliosides
Cells
Sialic Acids
Derivatives
G(M3) Ganglioside
COS Cells
Level control
Cell adhesion
Chemical modification
Carboxylic Acids
Oligosaccharides
Galactose
Cell Adhesion
Hydroxyl Radical

ASJC Scopus subject areas

  • Biochemistry

Cite this

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. / Collins, Brian E.; Kiso, Makoto; Hasegawa, Akira; Tropak, Michael B.; Roder, John C.; Crocker, Paul R.; Schnaar, Ronald Lee.

In: Journal of Biological Chemistry, Vol. 272, No. 27, 04.07.1997, p. 16889-16895.

Research output: Contribution to journalArticle

@article{29e687fcf4bb4949ab6254f195fdfb41,
title = "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",
abstract = "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 α2,3-linked sialic acid on the terminal galactose of a neutral saccharide core, and they shared the following rank-order potency of binding: G(Q1bα) >> 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 α2,3- or α2,8-linked sialic acids with the following rank- order potency of binding: G(Q1bα) > 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 acetamide 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.",
author = "Collins, {Brian E.} and Makoto Kiso and Akira Hasegawa and Tropak, {Michael B.} and Roder, {John C.} and Crocker, {Paul R.} and Schnaar, {Ronald Lee}",
year = "1997",
month = "7",
day = "4",
doi = "10.1074/jbc.272.27.16889",
language = "English (US)",
volume = "272",
pages = "16889--16895",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "27",

}

TY - JOUR

T1 - Binding specificities of the sialoadhesin family of I-type lectins

T2 - Sialic acid linkage and substructure requirements for binding of myelin- associated glycoprotein, Schwann cell myelin protein, and sialoadhesin

AU - Collins, Brian E.

AU - Kiso, Makoto

AU - Hasegawa, Akira

AU - Tropak, Michael B.

AU - Roder, John C.

AU - Crocker, Paul R.

AU - Schnaar, Ronald Lee

PY - 1997/7/4

Y1 - 1997/7/4

N2 - 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 α2,3-linked sialic acid on the terminal galactose of a neutral saccharide core, and they shared the following rank-order potency of binding: G(Q1bα) >> 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 α2,3- or α2,8-linked sialic acids with the following rank- order potency of binding: G(Q1bα) > 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 acetamide 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.

AB - 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 α2,3-linked sialic acid on the terminal galactose of a neutral saccharide core, and they shared the following rank-order potency of binding: G(Q1bα) >> 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 α2,3- or α2,8-linked sialic acids with the following rank- order potency of binding: G(Q1bα) > 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 acetamide 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.

UR - http://www.scopus.com/inward/record.url?scp=0030758770&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030758770&partnerID=8YFLogxK

U2 - 10.1074/jbc.272.27.16889

DO - 10.1074/jbc.272.27.16889

M3 - Article

C2 - 9201997

AN - SCOPUS:0030758770

VL - 272

SP - 16889

EP - 16895

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 27

ER -