Abstract
Our study deals with the interaction of CD33 related-siglecs-5,-7,-8,-9,-10 with gangliosides GT1b, GQ1b, GD3, GM2, GM3 and GD1a. Siglec-5 bound preferentially to GQ1b, but weakly to GT1b, whereas siglec-10 interacted only with GT1b ganglioside. Siglec-7 and siglec-9 displayed binding to gangliosides GD3, GQ1b and GT1b bearing a disialoside motif, though siglec-7 was more potent; besides, siglec-9 interacted also with GM3. Siglec-8 demonstrated low affinity to the gangliosides tested compared with other siglecs. Despite high structural similarity of CD33 related siglecs, they demonstrated different ganglioside selectivity, in particular to the Neu5Acalpha2-8Neu5Ac motif.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, CD / chemistry
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Antigens, CD / metabolism*
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Antigens, Differentiation, B-Lymphocyte
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Antigens, Differentiation, Myelomonocytic / chemistry
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Antigens, Differentiation, Myelomonocytic / metabolism*
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Carbohydrate Sequence
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G(M2) Ganglioside
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G(M3) Ganglioside
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Gangliosides / chemistry
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Gangliosides / metabolism*
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Humans
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Immunoenzyme Techniques
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Lectins
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Protein Binding
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Receptors, Cell Surface
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Sialic Acid Binding Ig-like Lectin 3
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Sialic Acid Binding Immunoglobulin-like Lectins
Substances
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Antigens, CD
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Antigens, Differentiation, B-Lymphocyte
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Antigens, Differentiation, Myelomonocytic
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CD33 protein, human
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G(M3) Ganglioside
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Gangliosides
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Lectins
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Receptors, Cell Surface
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SIGLEC10 protein, human
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SIGLEC5 protein, human
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SIGLEC7 protein, human
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SIGLEC8 protein, human
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SIGLEC9 protein, human
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Sialic Acid Binding Ig-like Lectin 3
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Sialic Acid Binding Immunoglobulin-like Lectins
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ganglioside, GD1a
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G(M2) Ganglioside
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trisialoganglioside GT1
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ganglioside, GD3
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GQ1b ganglioside