Characterization of new rat anti-mouse IgE monoclonals and their use along with chimeric IgE to further define the site that interacts with FcϵRII and FcϵRI

Keegan, Achsah; Fratazzi, Candida; Shopes, Bob; Baird, Barbara; Conrad, Daniel H.

doi:10.1016/0161-5890(91)90030-n

Cited by 53 publications

(39 citation statements)

References 22 publications

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“…4C). This was expected because, as mentioned above, sFcRI␣ blocks the binding of IgE to both receptors (11,56,57). We conclude that the binding of MOv18 IgE to both IgE receptors on monocytes contributed to IgE-mediated tumor cell targeting and killing.…”

Section: Up-regulation Of Fcri On Monocytes and Function In Ige Adcc mentioning

confidence: 73%

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IgE-Antibody-Dependent Immunotherapy of Solid Tumors: Cytotoxic and Phagocytic Mechanisms of Eradication of Ovarian Cancer Cells

Karagiannis

Bracher

Hunt

et al. 2007

The Journal of Immunology

100

124

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Abs have a paramount place in the treatment of certain, mainly lymphoid, malignancies, although tumors of nonhemopoietic origin have proved more refractory ones. We have previously shown that the efficacy of immunotherapy of solid tumors, in particular ovarian carcinoma, may be improved by the use of IgE Abs in place of the conventional IgG. An IgE Ab (MOv18 IgE) against an ovarian-tumor-specific Ag (folate binding protein), in combination with human PBMC, introduced into ovarian cancer xenograft-bearing mice, greatly exceeded the analogous IgG1 in promoting survival. In this study, we analyzed the mechanisms by which MOv18 IgE may exert its antitumor activities. Monocytes were essential IgE receptor-expressing effector cells that mediated the enhanced survival of tumor-bearing mice by MOv18 IgE and human PBMC. Monocytes mediated MOv18 IgE-dependent ovarian tumor cell killing in vitro by two distinct pathways, cytotoxicity and phagocytosis, acting respectively through the IgE receptors FcεRI and CD23. We also show that human eosinophils were potent effector cells in MOv18 IgE Ab-dependent ovarian tumor cell cytotoxicity in vitro. These results demonstrate that IgE Abs can engage cell surface IgE receptors and activate effector cells against ovarian tumor cells. Our findings offer a framework for an improved immunotherapeutic strategy for combating solid tumors.

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Section: Up-regulation Of Fcri On Monocytes and Function In Ige Adcc mentioning

confidence: 73%

“…This demonstrates that sFcRI␣ prevented binding of MOv18 IgE on the surface of monocytes. The binding sites of sFcRI and CD23 on IgE are competitive (11,56,57), so that sFcRI␣ in 100-fold molar excess must prevent the association of IgE to both receptors.…”

Section: Up-regulation Of Fcri On Monocytes and Function In Ige Adcc mentioning

confidence: 99%

IgE-Antibody-Dependent Immunotherapy of Solid Tumors: Cytotoxic and Phagocytic Mechanisms of Eradication of Ovarian Cancer Cells

Karagiannis

Bracher

Hunt

et al. 2007

The Journal of Immunology

100

124

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“…Data using peptides derived from the Fc region of IgE as well as mAbs directed against the Fc region of IgE indicated that the two IgE receptors interact with closely adjacent, but not identical, sites on the Fc region of IgE (11,12). Recent analysis of IgE-Fc/Fc⑀RI␣ crystals have confirmed that the interaction site for the Fc⑀RI is in the C⑀3 domain of IgE (13).…”

mentioning

confidence: 95%

Temperature Effect on IgE Binding to CD23 Versus FcεRI

Chen

Kilmon

et al. 2003

The Journal of Immunology

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A chimeric soluble CD23, consisting of the extracellular domain of mouse CD23 and a modified leucine zipper (lz-CD23), has been shown to inhibit IgE binding to the FcεRI. A similar human CD23 construct was also shown to inhibit binding of human IgE to human FcεRI. In both systems, the inhibition was found to be temperature dependent; a 10-fold molar excess of lz-CD23 gave 90–98% inhibition at 4°C, dropping to 20–30% inhibition at 37°C. Surface plasmon resonance analysis of lz-CD23 binding to an IgE-coated sensor chip suggested that the effective concentration of lz-CD23 was lower at the higher temperatures. Analysis of 125I-IgE binding to CD23+-Chinese hamster ovary cells also indicated that increased temperature resulted in a lower percentage of IgE capable of interacting with CD23. In contrast, IgE interacts more effectively with FcεRI+-rat basophilic leukemia cells at 37°C compared with 4°C. The results support the concept that the open and closed IgE structures found by crystallography interact differently with the two IgE receptors and suggest that temperature influences the relative percentage of IgE in the respective structural forms. Changes in CD23 oligomerization also plays a role in the decreased binding seen at physiological temperatures.

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“…Alternative anti-IgE monoclonal antibodies have been shown to detect only endogenous IgE molecules. The hybridoma clone R1E4 produces a rat-anti-mouse monoclonal IgE antibody specific only for endogenous surface molecules, not cytophilic IgE bound to CD23 21,22 , but is not commercially available. The protocol described above is convenient and economical because it uses common lab reagents.…”

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confidence: 99%

Detection of True IgE-expressing Mouse B Lineage Cells

Gallagher

Shrestha

Magee

et al. 2014

JoVE

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B lymphocyte immunoglobulin heavy chain (IgH) class switch recombination (CSR) is a process wherein initially expressed IgM switches to other IgH isotypes, such as IgA, IgE and IgG. Measurement of IgH CSR in vitro is a key method for the study of a number of biologic processes ranging from DNA recombination and repair to aspects of molecular and cellular immunology. In vitro CSR assay involves the flow cytometric measurement surface Ig expression on activated B cells. While measurement of IgA and IgG subclasses is straightforward, measurement of IgE by this method is problematic due to soluble IgE binding to FcεRII/CD23 expressed on the surface of activated B cells. Here we describe a unique procedure for accurate measurement of IgE-producing mouse B cells that have undergone CSR in culture. The method is based on trypsin-mediated cleavage of IgE-CD23 complexes on cell surfaces, allowing for detection of IgE-producing B lineage cells by cytoplasmic staining. This procedure offers a convenient solution for flow cytometric analysis of CSR to IgE. Video LinkThe video component of this article can be found at

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Characterization of new rat anti-mouse IgE monoclonals and their use along with chimeric IgE to further define the site that interacts with FcϵRII and FcϵRI

Cited by 53 publications

References 22 publications

IgE-Antibody-Dependent Immunotherapy of Solid Tumors: Cytotoxic and Phagocytic Mechanisms of Eradication of Ovarian Cancer Cells

IgE-Antibody-Dependent Immunotherapy of Solid Tumors: Cytotoxic and Phagocytic Mechanisms of Eradication of Ovarian Cancer Cells

Temperature Effect on IgE Binding to CD23 Versus FcεRI

Detection of True IgE-expressing Mouse B Lineage Cells

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