ArticleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2014
Human IgE against the major allergen Bet v 1--defining an epitope with limited cross-reactivity between different PR-10 family proteins.
Article in Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Insights into structural and binding studies of pollen allergen Bet v 1 using computational approaches.In silico pharmacology · 2025Article
- A genome-wide association study for allergen component sensitizations identifies allergen component-specific and allergen protein group-specific associations.The journal of allergy and clinical immunology. Global · 2023Article
- Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1.Foods (Basel, Switzerland) · 2021Article
- Filling the Antibody Pipeline in Allergy: PIPE Cloning of IgE, IgGInternational journal of molecular sciences · 2020Article
- Structural Aspects of the Allergen-Antibody Interaction.Frontiers in immunology · 2020Review
- Antibodies and superantibodies in patients with chronic rhinosinusitis with nasal polyps.The Journal of allergy and clinical immunology · 2017Article
- Antibody Heavy Chain Variable Domains of Different Germline Gene Origins Diversify through Different Paths.Frontiers in immunology · 2017Article
- Nanoparticle-allergen interactions mediate human allergic responses: protein corona characterization and cellular responses.Particle and fibre toxicology · 2016Article
- Isolation of Mal d 1 and Api g 1 - specific recombinant antibodies from mouse IgG Fab fragment libraries - Mal d 1-specific antibody exhibits cross-reactivity against Bet v 1.BMC biotechnology · 2015Article
- Interfaces between allergen structure and diagnosis: know your epitopes.Current allergy and asthma reports · 2015Article
- Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.Biophysical journal · 2014Article
- The human IgE repertoire.International archives of allergy and immunology · 2014Review
- Enlarging the toolbox for allergen epitope definition with an allergen-type model protein.PloS one · 2014Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundThe interaction between IgE and allergen is a key event at the initiation of an allergic response, and its characteristics have substantial effects on the clinical manifestation. Despite this, the molecular details of the interaction between human IgE and the major birch allergen Bet v 1, one of the most potent tree allergens, still remain poorly investigated.
objectiveTo isolate Bet v 1-specific human monoclonal IgE and characterize their interaction with the allergen.
methodsRecombinant human IgE were isolated from a combinatorial antibody fragment library and their interaction with Bet v 1 assessed using various immunological assays. The structure of one such IgE in the single-chain fragment variable format was determined using X-ray crystallography.
resultsWe present four novel Bet v 1-specific IgE, for one of which we solve the structure, all with their genetic origin in the IGHV5 germline gene, and demonstrate that they target two non-overlapping epitopes on the surface of Bet v 1, thereby fulfilling the basic criteria for FcεRI cross-linkage. We further define these epitopes and for one epitope pinpoint single amino acid residues important for the interaction with human IgE. This provides a potential explanation, at the molecular level, for the differences in recognition of isoforms of Bet v 1 and other allergens in the PR-10 protein family displayed by IgE targeting this epitope. Finally, we present the first high-resolution structure of a human allergen-specific IgE fragment in the single-chain fragment variable (scFv) format. CONCLUSIONS AND CLINICAL RELEVANCE: We here display the usefulness of allergen-specific human monoclonal IgE as a tool in studies of the crucial molecular interaction taking place at the initiation of an allergic response. Such studies may aid us in development of better diagnostic tools and guide us in the development of new therapeutic compounds.
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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.