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CD23 is a glycan-binding receptor in some mammalian species
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Title: | CD23 is a glycan-binding receptor in some mammalian species |
Authors: | Jégouzo, SAF Feinberg, H Morrison, A Holder, A May, A Huang, Z Jiang, L Lasanajak, Y Smith, DF Werling, D Drickamer, K Weis, WI Taylor, ME |
Item Type: | Journal Article |
Abstract: | 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, N-acetylglucosamine, 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 CD23 gene 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 micro-organisms 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. |
Issue Date: | 11-Oct-2019 |
Date of Acceptance: | 5-Sep-2019 |
URI: | http://hdl.handle.net/10044/1/74070 |
DOI: | https://dx.doi.org/10.1074/jbc.RA119.010572 |
ISSN: | 0021-9258 |
Publisher: | American Society for Biochemistry and Molecular Biology |
Start Page: | 14845 |
End Page: | 14859 |
Journal / Book Title: | Journal of Biological Chemistry |
Volume: | 294 |
Copyright Statement: | © 2019 Jégouzo et al. Author's Choice—Final version open access under the terms of the Creative Commons CC-BY license (https://creativecommons.org/licenses/by/4.0/) |
Sponsor/Funder: | Biotechnology and Biological Sciences Research Council (BBSRC) |
Funder's Grant Number: | BB/P005659/1 |
Keywords: | CLEC4J FCER2 gene Fc receptor carbohydrate function carbohydrate-binding protein carbohydrate-recognition domain crystal structure glycan-binding receptors glycobiology lectin CLEC4J FCER2 gene Fc receptor carbohydrate function carbohydrate-binding protein carbohydrate-recognition domain crystal structure glycan-binding receptors glycobiology lectin Biochemistry & Molecular Biology 06 Biological Sciences 11 Medical and Health Sciences 03 Chemical Sciences |
Publication Status: | Published |
Conference Place: | United States |
Online Publication Date: | 2019-09-05 |
Appears in Collections: | Faculty of Natural Sciences |