An anti-IgE monoclonal antibody that binds to IgE on CD23 but not on high-affinity IgE.Fc receptors

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• 作者：Yu-Yu Shiung^a ; ^b ; Chen-Yi Chiang^b ; Jiun-Bo Chen^b ; Pheidias C. Wu^a ; ^b ; Alfur Fu-Hsin Hung^a ; ^b ; Donic Chien-Sheng Lu^b ; Rong-Long Pan^a ; Tse Wen Chang^b ; ^{twchang@gate.sinica.edu.tw}
• 关键词：ELISA ; enzyme-linked immunosorbent assay ; FITC ; fluorescein isothiocyanate ; HRP ; horseradish peroxidase ; IgE ; immunoglobulin E ; mAb ; monoclonal antibody ; PEI ; polyethylenimine ; RT ; room temperature
• 刊名：Immunobiology
• 出版年：2012
• 期刊代码：3_01712985
• 类别：imm
• 出版时间：July, 2012
• 卷：217
• 期：7
• 页码：676-683
• 文件大小：814 K

摘要

A new monoclonal antibody (mAb), specific for human IgE, the central mediator of immediate-type hypersensitivity reactions, has been shown to possess a unique set of binding specificities. The mAb, 8D6, binds to a conformational epitope on the CH3 domain of human e immunoglobulin and can compete with omalizumab for binding to IgE. Like omalizumab, it does not bind to IgE bound by the high-affinity IgE.Fc receptor (Fc蓻RI) on basophils and mast cells. It also does not cause activation and degranulation of IgE-pulsed, human Fc蓻RI-expressing rat basophilic leukemic cells (RBL SX-38). The mAb can inhibit IgE binding to recombinant 伪 chain of human Fc蓻RI in ELISA and to human Fc蓻RI-expressing RBL SX38 cells in fluorescence flow cytometric analysis. However, unlike omalizumab, 8D6 can bind to IgE already bound by the low-affinity IgE.Fc receptors (Fc蓻RII, or CD23), as revealed in ELISA with recombinant CD23 and in flow cytometric analysis with human B cells. Since earlier investigators have shown that anti-CD23 mAbs can inhibit the synthesis of IgE in lymphocyte culture in vitro and can down-regulate IgE production in treated patients, 8D6 may offer pharmacological mechanisms in addition to those mediated by omalizumab, for controlling IgE in patients with allergic diseases.