Conformational plasticity at the IgE-binding site of the B-cell receptor CD23

Balvinder Dhaliwal; Marie O Y Pang; Daopeng Yuan; Norhakim Yahya; Stella M. Fabiane; James M. McDonnell; Hannah J. Gould; Andrew J. Beavil; Brian J. Sutton

doi:10.1016/j.molimm.2013.07.005

Conformational plasticity at the IgE-binding site of the B-cell receptor CD23

Balvinder Dhaliwal, Marie O Y Pang, Daopeng Yuan, Norhakim Yahya, Stella M. Fabiane, James M. McDonnell, Hannah J. Gould, Andrew J. Beavil, Brian J. Sutton

Research output: Contribution to journal › Article › peer-review

Abstract

IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, Fce{open}RI and CD23. Crosslinking of Fce{open}RI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding. © 2013 The Authors.

Original language	English
Pages (from-to)	693-697
Number of pages	4
Journal	Molecular immunology
Volume	56
Issue number	4
DOIs	https://doi.org/10.1016/j.molimm.2013.07.005
Publication status	Published - 31 Dec 2013

Keywords

Allergy
Antibody-receptor interactions
Immunoglobulin E
Immunology
X-ray crystallography

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.molimm.2013.07.005

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title = "Conformational plasticity at the IgE-binding site of the B-cell receptor CD23",

abstract = "IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, Fce{open}RI and CD23. Crosslinking of Fce{open}RI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin {"}head{"} domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding. {\textcopyright} 2013 The Authors.",

keywords = "Allergy, Antibody-receptor interactions, Immunoglobulin E, Immunology, X-ray crystallography",

author = "Balvinder Dhaliwal and Pang, {Marie O Y} and Daopeng Yuan and Norhakim Yahya and Fabiane, {Stella M.} and McDonnell, {James M.} and Gould, {Hannah J.} and Beavil, {Andrew J.} and Sutton, {Brian J.}",

note = "G0501494, Medical Research Council, United KingdomG1100090, Medical Research Council, United KingdomMR/J006742/1, Medical Research Council, United Kingdom, Medical Research Council, United Kingdom, Wellcome Trust, United Kingdom",

year = "2013",

month = dec,

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doi = "10.1016/j.molimm.2013.07.005",

language = "English",

volume = "56",

pages = "693--697",

journal = "Molecular immunology",

issn = "0161-5890",

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T1 - Conformational plasticity at the IgE-binding site of the B-cell receptor CD23

AU - Dhaliwal, Balvinder

AU - Pang, Marie O Y

AU - Yuan, Daopeng

AU - Yahya, Norhakim

AU - Fabiane, Stella M.

AU - McDonnell, James M.

AU - Gould, Hannah J.

AU - Beavil, Andrew J.

AU - Sutton, Brian J.

N1 - G0501494, Medical Research Council, United KingdomG1100090, Medical Research Council, United KingdomMR/J006742/1, Medical Research Council, United Kingdom, Medical Research Council, United Kingdom, Wellcome Trust, United Kingdom

PY - 2013/12/31

Y1 - 2013/12/31

N2 - IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, Fce{open}RI and CD23. Crosslinking of Fce{open}RI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding. © 2013 The Authors.

AB - IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, Fce{open}RI and CD23. Crosslinking of Fce{open}RI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding. © 2013 The Authors.

KW - Allergy

KW - Antibody-receptor interactions

KW - Immunoglobulin E

KW - Immunology

KW - X-ray crystallography

U2 - 10.1016/j.molimm.2013.07.005

DO - 10.1016/j.molimm.2013.07.005

M3 - Article

C2 - 23933509

SN - 0161-5890

VL - 56

SP - 693

EP - 697

JO - Molecular immunology

JF - Molecular immunology

IS - 4

ER -

Conformational plasticity at the IgE-binding site of the B-cell receptor CD23

Abstract

Keywords

UN SDGs

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