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Humanized IgE/FcepsilonR1 Mouse

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Strain Background: C57BL/6N

 

hIgE/hFcεR1 Features:

  •   Human IgE immunoglobulin and no mouse IgE immunoglobulin (Fig. 1B), human FcεRI receptor and no mouse FcεRI receptor (Fig. 1A).
  •   FcεR1 receptor is expressed under the control of the minimum human promoter to mimic the human pattern of expression. The cell distribution of hFcεR1 in mice is comparable to that of humans (expressed in mast cells, basophils, monocytes/dendritic cells, Langerhans cells, and eosinophils).
  •    The human-mouse chimeric IgE/FcεR1 complex (humanization of the protein domain of the IgE/FcεR1 binding region; humanization of the IgE Fc end and FcεR1 α-chain) has a normal physiological expression and regulation pattern, retaining the mouse IgE Fab end and FcεR1 β and γ chains (does not require mutual binding domains).

 

Research & Application:

The humanized IgE/FcεR1 mouse model has been successfully used to screen for innovative therapeutics for allergy, asthma and other IgE-mediated diseases (Eosinophilic esophagitis and inflammatory bowel disease).

 

Validation Data:

A major limit for in vivo studies is the different cellular distribution of the IgE high-affinity receptor. In mice, the IgE high-affinity receptor is not expressed on monocytes/DCs, Langerhans cells, or eosinophils whereas it is in humans. The model enables the production of a fully human IgE-FcεRI complex combined with a human-like expression of a FcεRI receptor.

Figure 1. Analysis of human FcεR1 and human IgE expression in double humanized IgE/FcεR1 mouse cells. a) Expression of hFcεR1-α chain from bone marrow-derived mast cells cultured in presence of murine IL3, SCF, and IL6 for 8 weeks. b) Human IgE in serum of mice sensitized and challenged with ovalbumin. (black column: treated; white column: untreated)

Figure 2. Functional data on double humanized IgE/FcεR1 model: Induction of mast cell degranulation by anti-IgE Ab. Mast cells were sensitized with human IgE overnight to load hFcεR1 receptors and degranulation was stimulated by cross-linking loaded receptors with anti-hIgE. β-hexosaminidase activity in cell supernatant was determined as a percentage of total β-hexosaminidase activity in cell lysates.
Conclusion: Mast cells from the humanized model bind human IgE and degranulate upon cross-linking. This is specific and not restricted to given antigen. This set of data validates the functionality of the IgE high-affinity receptor. It binds human IgE and triggers degranulation upon cross-linking.

Figure 3. Functional data on double humanized IgE/FcεRI model: Inhibition of mast cell degranulation by anti-IgE monoclonal Ab. Mast cells were sensitized overnight with human IgE in presence of indicated biologics. The cells were washed and stimulated with anti-IgE. β-hexosaminidase activity in cell supernatant was determined as a percentage of total β-hexosaminidase activity in cell lysates.
Conclusion: Anti-IgE Ab, but not the isotype control, suppresses hFcεR1-mediated degranulation in a dose-dependent manner.

Figure 4. Expression of hFcεR1 in humanized IgE/FcεR1 mouse cells. (Left) The expression of hFcεR1α chain was detected on mast cells (BMMCs) derived from mouse bone marrow stimulated by IL-3, stem cell factor (SCF) and IL-6 (8 weeks of treatment). (Right) hFcεR1 mice were injected intravenously with eotaxin (2.4nmol/kg), and hFcεR1 expression was detected in peripheral blood eosinophils.

Figure 5. The functional data of the humanized IgE/FcεR1 mouse model. (Left) After binding to hFcεR1, IgE triggers the degranulation of mast cells. (Right) Mast cells respond to hFcεR1, but do not respond to mFcεR1 cross-linking (XL).

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