CD23 is a glycan-binding receptor in some mammalian species.

Autor:	Jégouzo SAF; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom., Feinberg H; Departments of Structural Biology and Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305., Morrison AG; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom., Holder A; Department of Pathobiology and Population Sciences, Royal Veterinary College, North Mymms, Hatfield, Hertfordshire AL9 7TA, United Kingdom., May A; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom., Huang Z; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom., Jiang L; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom., Lasanajak Y; Emory Comprehensive Glycomics Core, Emory University School of Medicine, Atlanta, Georgia 30322., Smith DF; Emory Comprehensive Glycomics Core, Emory University School of Medicine, Atlanta, Georgia 30322., Werling D; Department of Pathobiology and Population Sciences, Royal Veterinary College, North Mymms, Hatfield, Hertfordshire AL9 7TA, United Kingdom., Drickamer K; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom., Weis WI; Departments of Structural Biology and Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305., Taylor ME; Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom maureen.taylor@imperial.ac.uk.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2019 Oct 11; Vol. 294 (41), pp. 14845-14859. Date of Electronic Publication: 2019 Sep 05.
DOI:	10.1074/jbc.RA119.010572
Abstrakt:	CD23, the low-affinity IgE receptor found on B lymphocytes and other cells, contains a C-terminal lectin-like domain that resembles C-type carbohydrate-recognition domains (CRDs) found in many glycan-binding receptors. In most mammalian species, the CD23 residues required to form a sugar-binding site are present, although binding of CD23 to IgE does not involve sugars. Solid-phase binding competition assays, glycoprotein blotting experiments, and glycan array analysis employing the lectin-like domains of cow and mouse CD23 demonstrate that they bind to mannose, GlcNAc, glucose, and fucose and to glycoproteins that bear these sugars in nonreducing terminal positions. Crystal structures of the cow CRD in the presence of α-methyl mannoside and GlcNAcβ1-2Man reveal that a range of oligosaccharide ligands can be accommodated in an open binding site in which most interactions are with a single terminal sugar residue. Although mouse CD23 shows a pattern of monosaccharide and glycoprotein binding similar to cow CD23, the binding is weaker. In contrast, no sugar binding was observed in similar experiments with human CD23. The absence of sugar-binding activity correlates with accumulation of mutations in the gene for CD23 in the primate lineage leading to humans, resulting in loss of key sugar-binding residues. These results are consistent with a role for CD23 in many species as a receptor for potentially pathogenic microorganisms as well as IgE. However, the ability of CD23 to bind several different ligands varies between species, suggesting that it has distinct functions in different organisms. (© 2019 Jégouzo et al.)
Databáze:	MEDLINE
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