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offered its recent standing as a potential anti-IgE therapeutic and successor to omalizumab, we sought to analyze the IgE binding features of ligelizumab and its modes-of-motion. Here, we report the crystal framework of ligelizumab bound to IgE, revealing that it acknowledges a definite IgE epitope only partly overlapping with that of omalizumab. Ligelizumab interacts over the IgE-Fc dimer and favors the recognition of IgE within an open conformation different from its FcεRI- or CD23-certain conformations. What's more, it binds IgE with noticeably larger affinity than omalizumab and shows a correspondingly enhanced inhibition of IgE binding to FcεRI and basophil activation. In distinction and Irrespective of its higher affinity for IgE, ligelizumab is inferior to omalizumab in avoiding IgE binding to CD23.
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CD23 interacts with IgE-Fc with the hinge area concerning Cε3 and Cε4 domains (Fig. 2j), favoring a shut conformation of Cεthree domains34. Comparison of the CD23 and ligelizumab interaction web-sites on IgE indicates rather minimal overlap between binding web pages of these two IgE ligands (Fig. 2k). On top of that, the orientation in the ligelizumab VHVL domains on IgE (Fig. 2g) indicates that the ligelizumab Fab would venture from the IgE and wouldn't sterically overlap bound CD23, suggesting that Opposition for IgE floor subsites as well as the stabilization of an open Cε3 conformation would be the principal system of CD23 inhibition.