دورية أكاديمية
أعرض في EDS

Allosteric inhibition of IgE-FcεRI interactions by simultaneous targeting of IgE F(ab')2 epitopes.

التفاصيل البيبلوغرافية
العنوان: Allosteric inhibition of IgE-FcεRI interactions by simultaneous targeting of IgE F(ab')2 epitopes.
المؤلفون: Hirano T; Department of Hematology, Juntendo University Nerima Hospital, Nerima-ku, Tokyo, Japan. thirano@juntendo.ac.jp., Koyanagi A; Laboratory of Cell Biology, Biomedical Research Core Facilities, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan., Ago H; Advanced Photon Technology Division, RIKEN SPring-8 Center, Sayo, Hyogo, Japan., Yamamoto M; Advanced Photon Technology Division, RIKEN SPring-8 Center, Sayo, Hyogo, Japan., Kitaura J; Atopy Research Center, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan.; Department of Science of Allergy and Inflammation, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan., Kasai M; Atopy Research Center, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan., Okumura K; Atopy Research Center, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan.
المصدر: Communications biology [Commun Biol] 2024 Aug 23; Vol. 7 (1), pp. 1042. Date of Electronic Publication: 2024 Aug 23.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Nature Publishing Group UK Country of Publication: England NLM ID: 101719179 Publication Model: Electronic Cited Medium: Internet ISSN: 2399-3642 (Electronic) Linking ISSN: 23993642 NLM ISO Abbreviation: Commun Biol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: London, United Kingdom : Nature Publishing Group UK, [2018]-
مواضيع طبية MeSH: Immunoglobulin E*/immunology , Immunoglobulin E*/metabolism , Receptors, IgE*/immunology , Receptors, IgE*/metabolism , Immunoglobulin Fab Fragments*/immunology , Immunoglobulin Fab Fragments*/metabolism , Immunoglobulin Fab Fragments*/chemistry , Epitopes*/immunology, Animals ; Allosteric Regulation ; Crystallography, X-Ray ; Mice ; Protein Binding ; Mice, Inbred BALB C ; Antibodies, Anti-Idiotypic/immunology ; Antibodies, Anti-Idiotypic/chemistry ; Humans ; Anaphylaxis/immunology
مستخلص: Immunoglobulin E (IgE) plays pivotal roles in allergic diseases through interaction with a high-affinity receptor (FcεRI). We established that Fab fragments of anti-IgE antibodies (HMK-12 Fab) rapidly dissociate preformed IgE-FcεRI complexes in a temperature-dependent manner and inhibit IgE-mediated anaphylactic reactions, even after allergen challenge. X-ray crystallographic studies revealed that HMK-12 Fab interacts with each of two equivalent epitopes on the Cε2 homodimer domain involved in IgE F(ab')2. Consequently, HMK-12 Fab-mediated targeting of Cε2 reduced the binding affinity of Fc domains and resulted in rapid removal of IgE from the receptor complex. This unexpected finding of allosteric inhibition of IgE-FcεRI interactions by simultaneous targeting of two epitope sites on the Cε2 homodimer domain of IgE F(ab')2 may have implications for the development of novel therapies for allergic disease.
(© 2024. The Author(s).)
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معلومات مُعتمدة: 21K08447 Japan Society for the Promotion of Science London (JSPS London); JP21am0101070 Japan Agency for Medical Research and Development (AMED)
المشرفين على المادة: 37341-29-0 (Immunoglobulin E)
0 (Receptors, IgE)
0 (Immunoglobulin Fab Fragments)
0 (Epitopes)
0 (anti-IgE antibodies)
0 (Antibodies, Anti-Idiotypic)
تواريخ الأحداث: Date Created: 20240823 Date Completed: 20240823 Latest Revision: 20240826
رمز التحديث: 20240827
مُعرف محوري في PubMed: PMC11343869
DOI: 10.1038/s42003-024-06633-4
PMID: 39179708
قاعدة البيانات: MEDLINE
الوصف
تدمد:2399-3642
DOI:10.1038/s42003-024-06633-4