Allergen capture by IgE and IgG enhanced cell-binding by allergen multimers: How complex is it?
Collins, Andrew M. & Davies, Janet M. (2013) Allergen capture by IgE and IgG enhanced cell-binding by allergen multimers: How complex is it? Immunology and Cell Biology, 91(2), pp. 115-117.
Allergic diseases are the most common chronic disease of the western world, costing $7.8 billion per year in lost productivity and medical care in Australia alone.1 IgE is central to the immunopathogenesis of allergic diseases and important advances are now being made on multiple fronts of IgE research. In particular, two groups independently invested in the generation of IgE reporter mice to address the vexing question of the route of development of the elusive IgE+ B cell.2, 3 Two new anti-IgE mAb targeting membrane IgE and cell-bound IgE have the potential to deplete the cellular source of IgE.4, 5 These could be candidates for alternative anti-IgE treatment options with advantages over current anti-IgE therapy (OmalizumAb), which depletes free serum IgE. Researchers are still intrigued by the modes of interaction of IgE with allergen, and with both its receptors; the high affinity FcεR1 on mast cells and basophils, and the low affinity, C-type lectin, IgE receptor, CD23,6 on B cells and monocytes (Figure 1a and b). A new approach to the study of the complexity of these interactions was recently reported by Reginald et al.7 on page 167 of this issue.
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|Item Type:||Journal Article|
|Keywords:||fc-gamma-riib, b-cells, in-vivo, antibodies|
|Copyright Owner:||Copyright 2013 Nature Publishing Group|
|Deposited On:||01 Oct 2015 05:12|
|Last Modified:||02 Oct 2015 01:15|
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