دورية أكاديمية
أعرض في EDS

Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.

التفاصيل البيبلوغرافية
العنوان: Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.
المؤلفون: Chen JB; Genomics Research Center, Academia Sinica, Taipei, 115, Taiwan.; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom., Ramadani F; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom., Pang MOY; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom., Beavil RL; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma Protein Production Facility, London, United Kingdom., Holdom MD; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom., Mitropoulou AN; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom., Beavil AJ; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom., Gould HJ; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom., Chang TW; Genomics Research Center, Academia Sinica, Taipei, 115, Taiwan., Sutton BJ; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom. brian.sutton@kcl.ac.uk.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom. brian.sutton@kcl.ac.uk., McDonnell JM; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom. james.mcdonnell@kcl.ac.uk.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom. james.mcdonnell@kcl.ac.uk., Davies AM; King's College London, Randall Centre for Cell and Molecular Biophysics, London, SE1 1UL, United Kingdom. anna.davies@kcl.ac.uk.; Medical Research Council & Asthma UK Centre in Allergic Mechanisms of Asthma, London, United Kingdom. anna.davies@kcl.ac.uk.
المصدر: Scientific reports [Sci Rep] 2018 Aug 01; Vol. 8 (1), pp. 11548. Date of Electronic Publication: 2018 Aug 01.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London : Nature Publishing Group, copyright 2011-
مواضيع طبية MeSH: Antibodies, Anti-Idiotypic/*chemistry , Antibodies, Anti-Idiotypic/*metabolism , Immunoglobulin E/*chemistry , Immunoglobulin E/*metabolism , Receptors, IgE/*metabolism, B-Lymphocytes/immunology ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Fab Fragments/metabolism ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/metabolism ; Mast Cells/immunology ; Protein Binding ; Protein Conformation
مستخلص: Immunoglobulin E (IgE) antibodies play a central role in the allergic response: interaction with FcεRI on mast cells and basophils leads to immediate hypersensitivity reactions upon allergen challenge, while interaction with CD23/FcεRII, expressed on a variety of cells, regulates IgE synthesis among other activities. The receptor-binding IgE-Fc region has recently been found to display remarkable flexibility, from acutely bent to extended conformations, with allosteric communication between the distant FcεRI and CD23 binding sites. We report the structure of an anti-IgE antibody Fab (8D6) bound to IgE-Fc through a mixed protein-carbohydrate epitope, revealing further flexibility and a novel extended conformation with potential relevance to that of membrane-bound IgE in the B cell receptor for antigen. Unlike the earlier, clinically approved anti-IgE antibody omalizumab, 8D6 inhibits binding to FcεRI but not CD23; the structure reveals how this discrimination is achieved through both orthosteric and allosteric mechanisms, supporting therapeutic strategies that retain the benefits of CD23 binding.
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معلومات مُعتمدة: G1100090 International Medical Research Council (MRC); 085944 United Kingdom WT_ Wellcome Trust; AUK-PG-2013-183 International Asthma UK; G1100090 United Kingdom MRC_ Medical Research Council; United Kingdom WT_ Wellcome Trust
المشرفين على المادة: 0 (Antibodies, Anti-Idiotypic)
0 (Immunoglobulin Fab Fragments)
0 (Immunoglobulin Fc Fragments)
0 (Receptors, IgE)
0 (anti-IgE antibodies)
37341-29-0 (Immunoglobulin E)
تواريخ الأحداث: Date Created: 20180803 Date Completed: 20191021 Latest Revision: 20230926
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC6070508
DOI: 10.1038/s41598-018-29664-4
PMID: 30069035
قاعدة البيانات: MEDLINE
الوصف
تدمد:2045-2322
DOI:10.1038/s41598-018-29664-4