ArticleActa crystallographica. Section F, Structural biology communications2015
Structure of the omalizumab Fab.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Influence of genetic polymorphisms on omalizumab clinical response in pediatric severe asthma: a pilot study.Frontiers in pharmacology · 2026Article
- Efficacy of omalizumab after discontinuation: a retrospective single-center observational study in children with severe asthma.Frontiers in allergy · 2025Article
- Common framework mutations impact antibody interfacial dynamics and flexibility.Frontiers in immunology · 2023Article
- Regulatory Approved Monoclonal Antibodies Contain Framework Mutations Predicted From Human Antibody Repertoires.Frontiers in immunology · 2021Article
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Immunoglobulin G; structure and functional implications of different subclass modifications in initiation and resolution of allergy.Immunity, inflammation and disease · 2018Review
- Pediatric severe asthma: a case series report and perspectives on anti-IgE treatment.BMC pediatrics · 2018Review
- Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab.The Journal of biological chemistry · 2017Article
- Critical and direct involvement of the CD23 stalk region in IgE binding.The Journal of allergy and clinical immunology · 2017Article
- Structural basis of omalizumab therapy and omalizumab-mediated IgE exchange.Nature communications · 2016Article
- Monoclonal antibodies: the new magic bullets for allergy: IUPHAR Review 17.British journal of pharmacology · 2016Review
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Omalizumab is a humanized anti-IgE antibody that inhibits the binding of IgE to its receptors on mast cells and basophils, thus blocking the IgE-mediated release of inflammatory mediators from these cells. Omalizumab binds to the Fc domains of IgE in proximity to the binding site of the high-affinity IgE receptor FcℇRI, but the epitope and the mechanisms and conformations governing the recognition remain unknown. In order to elucidate the molecular mechanism of its anti-IgE activity, the aim was to analyse the interaction of omalizumab with human IgE. Therefore, IgE Fc Cℇ2-4 was recombinantly produced in mammalian HEK-293 cells. Functionality of the IgE Fc was proven by ELISA and mediator-release assays. Omalizumab IgG was cleaved with papain and the resulting Fab was purified by ion-exchange chromatography. The complex of IgE Fc with omalizumab was prepared by size-exclusion chromatography. However, crystals containing the complex were not obtained, suggesting that the process of crystallization favoured the dissociation of the two proteins. Instead, two structures of the omalizumab Fab with maximum resolutions of 1.9 and 3.0 Å were obtained. The structures reveal the arrangement of the CDRs and the position of omalizumab residues known from prior functional studies to be involved in IgE binding. Thus, the structure of omalizumab provides the structural basis for understanding the function of omalizumab, allows optimization of the procedure for complex crystallization and poses questions about the conformational requirements for anti-IgE activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.