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Table of Contents
Vol. 128, No. 4, 2002
Issue release date: August 2002
Section title: Original Paper
Int Arch Allergy Immunol 2002;128:315–324
(DOI:10.1159/000063860)

Monoclonal Antibodies against the CεmX Domain of Human Membrane-Bound IgE and Their Potential Use for Targeting IgE-Expressing B Cells

Chen H.Y.a,b · Liu F.-T.b · Hou C.M.H.a · Huang J.S.W.a · Sharma B.B.b · Chang T.W.a
aDepartment of Life Science, National Tsing Hua University, Hsinchu, Taiwan, ROC; bLa Jolla Institute for Allergy and Immunology, San Diego, Calif., USA

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: November 06, 2001
Accepted: May 02, 2002
Published online: September 06, 2002
Issue release date: August 2002

Number of Print Pages: 10
Number of Figures: 8
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA

Abstract

Background: IgE mediates immediate-type hypersensitivity reactions responsible for various allergic symptoms. It is secreted by IgE-producing plasma cells, which differentiate from B cells expressing membrane-bound IgE (mIgE) on their surface. The Ε-chain of human mIgE contains a membrane-anchoring peptide and an extra 52-amino-acid (a.a.)-long domain (referred to as CΕmX) between the membrane anchor and the CH4 domain. Objective: The study was designed to evaluate the effects of CΕmX-specific monoclonal antibodies (mAbs) to target IgE-expressing B cells and decrease IgE production. Methods: A CΕmX-containing IgG1.Fc fusion protein was produced in CHO cells and used to immunize mice; five hybridoma clones secreting CΕmX-specific mAbs were obtained. Results: Characterization of the mAbs using ELISA, immunoprecipitation, and immunoblotting methods showed that they could bind to both native and denatured forms of CΕmX. The mAbs exhibited mutual inhibition of binding to mIgE. Epitope mapping using synthetic peptides revealed that all five mAbs recognize the same epitope, RADWPGPP, located near the C-terminus of CΕmX . Binding of one of the mAbs to mIgE on SKO-007 cells induced the cross-linking of mIgE molecules on the cell surface, resulting in their patching and capping. In vitro functional analysis revealed that mAbs are able to cause complement-mediated cytotoxicity on transfectants expressing the Fc portion of mIgE. Conclusion: We have prepared several human mIgE-specific mAbs. The potential of the mAbs on targeting mIgE+ B cells was demonstrated by CDC analysis.

© 2002 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: November 06, 2001
Accepted: May 02, 2002
Published online: September 06, 2002
Issue release date: August 2002

Number of Print Pages: 10
Number of Figures: 8
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: http://www.karger.com/IAA


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Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
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