Imperial College London
Alternate

ProfessorKurtDrickamer

Faculty of Natural Sciences, Department of Life Sciences

Chair in Biochemistry
 
 
 
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Contact

 

+44 (0)20 7594 5282k.drickamer

 
 
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Location

 

606Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Jégouzo:2019:10.1074/jbc.RA119.010572,
author = {Jégouzo, SAF and Feinberg, H and Morrison, A and Holder, A and May, A and Huang, Z and Jiang, L and Lasanajak, Y and Smith, DF and Werling, D and Drickamer, K and Weis, WI and Taylor, ME},
doi = {10.1074/jbc.RA119.010572},
journal = {Journal of Biological Chemistry},
pages = {14845--14859},
title = {CD23 is a glycan-binding receptor in some mammalian species},
url = {http://dx.doi.org/10.1074/jbc.RA119.010572},
volume = {294},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Jégouzo,SAF
AU  - Feinberg,H
AU  - Morrison,A
AU  - Holder,A
AU  - May,A
AU  - Huang,Z
AU  - Jiang,L
AU  - Lasanajak,Y
AU  - Smith,DF
AU  - Werling,D
AU  - Drickamer,K
AU  - Weis,WI
AU  - Taylor,ME
DO  - 10.1074/jbc.RA119.010572
EP  - 14859
PY  - 2019///
SN  - 0021-9258
SP  - 14845
TI  - CD23 is a glycan-binding receptor in some mammalian species
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.RA119.010572
UR  - https://www.ncbi.nlm.nih.gov/pubmed/31488546
UR  - http://hdl.handle.net/10044/1/74070
VL  - 294
ER  -
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