Inhibition of an in Vivo Antigen-Specific IgE Response by Antibodies to CD23

Flores‐Romo, Leopoldo; Shields, John G.; Humbert, Yves; Graber, Pierre; Aubry, Jean‐Pierre; Gauchat, Jean‐François; Ayala, Guidon; Allet, Bernard; Chávez, M.E. Flores; Bazin, Hervé; Capron, Moníque; Bonnefoy, Jean‐Yves

doi:10.1126/science.8351517

Cited by 110 publications

(47 citation statements)

References 30 publications

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“…Specific IgE antibody titers were increased and sustained in CD23-deficient mice as compared with controls (3). Anti-CD23 antibody (␣CD23) treatment of rats inhibited antigen-specific IgE immune response by 90% (4). Human in vitro IgE production was also inhibited by monoclonal ␣CD23, an effect that was shown to require the Fc␥ domain, as F(abЈ) 2 ␣CD23 was ineffective (5).…”

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confidence: 97%

Inhibition of Interleukin-4-induced Class Switch Recombination by a Human Immunoglobulin Fcγ-Fcϵ Chimeric Protein

Yamada

Zhu²,

Zhang³

et al. 2003

Journal of Biological Chemistry

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Immunoglobulin E (IgE) is important in mediating human allergic diseases. We tested the hypothesis that a human Ig Fc␥-Fc⑀ bifunctional chimeric protein, GE2, would inhibit IgE class switch recombination (CSR) by co-aggregating B-cell CD32 and CD23. Indeed, GE2 directly inhibited ⑀ germ-line transcription, subsequent CSR to ⑀ and IgE protein production. This CSR inhibition was dependent on CD23 binding and the phosphorylation of extracellular signal-related kinase (ERK), and it was mediated via suppression of interleukin-4-induced STAT6 phosphorylation. Treatment with PD98059, a specific inhibitor of mitogen-activated protein kinase kinase 1 (MAPKK1 (MEK1)) and MEK2 reversed the ability of GE2 to decrease CSR and STAT6 phosphorylation. GE2 stimulation induced ERK phosphorylation, whereas it did not alter the phosphorylation of c-Jun N-terminal kinase or p38 MAPK. The ability of GE2 to block human isotype switching to ⑀, in addition to its already demonstrated ability to inhibit mast cell and basophil function, suggests that it will provide an important novel benefit in the treatment of IgE-mediated diseases.

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confidence: 97%

Inhibition of Interleukin-4-induced Class Switch Recombination by a Human Immunoglobulin Fcγ-Fcϵ Chimeric Protein

Yamada

Zhu²,

Zhang³

et al. 2003

Journal of Biological Chemistry

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“…Anti-CD23 antibody treatment of rats inhibits antigen-specific IgE production (11), and treatment of allergen-sensitized mice with anti-CD23 antibody before airway allergen challenge reduces pulmonary eosinophil infiltration (12).…”

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confidence: 99%

Allergic airway sensitization induces T cell activation but not airway hyperresponsiveness in B cell-deficient mice

Hamelmann

Vella

Oshiba

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

126

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B cells play an important role in the allergic response by producing allergen-specific Igs as well as by serving as antigen-presenting cells. We studied the involvement of B cells in the development of responses in a murine model of allergic airway sensitization. Normal and B celldeficient ( Mt ؊͞؊ ) B10.BR mice were sensitized via the airways to ovalbumin; Ig production, cytokine elaboration from local lymph node cells, development of airway hyperresponsiveness, and histological changes in the airways were evaluated. Both strains of mice had increased production of T helper 2-like cytokines and developed an accumulation of eosinophils in the bronchial tissue after airway sensitization. However, only wild-type mice produced allergen-specific antibodies and exhibited altered airway function. B cell-deficient mice reconstituted with anti-ovalbumin IgE during the course of sensitization developed increases in airway responsiveness. These results indicated that neither B cells nor IgE were necessary for the induction of a T helper 2-type cytokine response or eosinophil infiltration of the airways after allergic sensitization but that IgE was required as a second signal for the development of airway hyperresponsiveness in this model of airway sensitization.

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“…The modulatory effect of CD23 on IgE synthesis has been demonstrated in animals treated with CD23 antibody (14) and in those genetically deficient in CD23 (15)(16)(17).…”

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Binding of Anti-CD23 Monoclonal Antibody to the Leucine Zipper Motif of FcεRII/CD23 on B Cell Membrane Promotes Its Proteolytic Cleavage

Munoz

Brignone

Grenier-Brossette³

et al. 1998

Journal of Biological Chemistry

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In the present study we have compared the binding of two monoclonal antibodies to CD23, EBVCS1 and mAb25, which recognize the stalk and the lectin domain, respectively, on the CD23 molecule. At 4°C, EBVCS1 binds to about 10% of the receptors recognized by mAb25 on the B cell surface. At 37°C, whereas mAb25 reaches its maximal binding within a few seconds, EB-VCS1 requires 60 min to bind to the same extent. Stabilization of the oligomeric structure of CD23 with IgE strongly affects in a dose-dependent fashion the number of binding sites seen by EBVCS1 but not the t 1/2 to reach them, suggesting that EBVCS1 binds to the coiled coil region through an allosteric mechanism. EBVCS1 rapidly down-modulates the membrane CD23 expression with a coincident increase of CD23-soluble fragments in the culture medium, an effect that is inhibited by IgE. In contrast, mAb25, as well as IgE, protects CD23 from proteolytic cleavage and stimulates its endocytosis. These results suggest that EBVCS1 unravels the coiled coil structure of CD23, rendering it more susceptible to proteolytic attack. This supports the oligomeric model proposed previously (Gould, H., Sutton, B., Edmeades, R., and Beavil, A. (1991) Monogr. Allergy 29, 28 -49). The biological significance of these observations is discussed.

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Inhibition of an in Vivo Antigen-Specific IgE Response by Antibodies to CD23

Cited by 110 publications

References 30 publications

Inhibition of Interleukin-4-induced Class Switch Recombination by a Human Immunoglobulin Fcγ-Fcϵ Chimeric Protein

Inhibition of Interleukin-4-induced Class Switch Recombination by a Human Immunoglobulin Fcγ-Fcϵ Chimeric Protein

Allergic airway sensitization induces T cell activation but not airway hyperresponsiveness in B cell-deficient mice

Binding of Anti-CD23 Monoclonal Antibody to the Leucine Zipper Motif of FcεRII/CD23 on B Cell Membrane Promotes Its Proteolytic Cleavage

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