The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22.

Journal article

Sialoadhesin and CD22 are members of a recently characterized family of sialic acid-dependent adhesion molecules belonging to the immunoglobulin superfamily. Sialoadhesin is a macrophage-restricted receptor containing 17 extracellular Ig-like domains which recognizes oligosaccharides terminating in NeuAc alpha 2-3Gal in N- and O-linked glycans. CD22 is a B cell-restricted receptor with seven Ig-like domains which selectively recognizes oligosaccharides terminating in NeuAc alpha 2-6Gal in N-g...

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Authors: Nath, D; Van Der Merwe, P; Kelm, S; Bradfield, P; Crocker, P

• Journal: Journal of biological chemistry
• Volume: 270
• Issue: 44
• Pages: 26184-26191
• Publication date: 1995-11-01
• DOI: 10.1074/jbc.270.44.26184
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Membrane Glycoproteins; Humans; Immunoglobulin Fc Fragments; Polymerase Chain Reaction; Amino Acid Sequence; Immunoglobulin G; Recombinant Fusion Proteins; Antibodies, Monoclonal; Sequence Homology, Amino Acid; Base Sequence; Antigens, Differentiation, B-Lymphocyte; Sialic Acids; Cell Adhesion; Antigens, CD; Animals; DNA Primers; Antigens, CD22; Cell Adhesion Molecules; Immunoglobulins; Carbohydrate Sequence; Receptors, Immunologic; Rats; Lectins; Epitopes; Mice; Molecular Sequence Data; Binding Sites