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CD23 is a glycan-binding receptor in some mammalian species

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J. Biol. Chem.-2019-Jégouzo-14845-59.pdfPublished version4.46 MBAdobe PDFView/Open
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