ArticleClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology2014
Multiple independent IgE epitopes on the highly allergenic grass pollen allergen Phl p 5.
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.
- Molecular Biomarkers in IgE Immunoassays Used for Grass Pollen Allergy Diagnosis in European Clinical Settings.International journal of molecular sciences · 2026Review
- Allergen-specific human IgE isolated through an allergen-agnostic pipeline-understanding immune response and allergen recognition.Communications biology · 2026Article
- Low nanomolar affinity to major grass pollen allergen Phl p 5 as achieved in an unmutated human antibody-lineage ancestor.Frontiers in immunology · 2025Article
- Microarray-based evaluation of selected recombinant timothy grass allergens expressed in E. Coli and N. Benthamiana.BMC biotechnology · 2024Article
- Factors predicting the outcome of allergen-specific nasal provocation test in children with grass pollen allergic rhinitis.Frontiers in allergy · 2023Article
- Review
- Linear Epitope Binding Patterns of Grass Pollen-Specific Antibodies in Allergy and in Response to Allergen-Specific Immunotherapy.Frontiers in allergy · 2022Article
- Review: The Nose as a Route for Therapy. Part 2 Immunotherapy.Frontiers in allergy · 2021Review
- Mapping Human Monoclonal IgE Epitopes on the Major Dust Mite Allergen Der p 2.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Structural Aspects of the Allergen-Antibody Interaction.Frontiers in immunology · 2020Review
- Interplay between Affinity and Valency in Effector Cell Degranulation: A Model System with Polcalcin Allergens and Human Patient-Derived IgE Antibodies.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- Grass pollen production and group V allergen content of agriculturally relevant species and cultivars.PloS one · 2018Article
- Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundGroup 5 allergens are small proteins that consist of two domains. They belong to the most potent respiratory allergens.
objectiveTo determine the binding sites and to study allergic patients' IgE recognition of the group 5 allergen (Phl p 5) from timothy grass pollen using human monoclonal IgE antibodies that have been isolated from grass pollen allergic patients.
methodsUsing recombinant isoallergens, fragments, mutants and synthetic peptides of Phl p 5, as well as peptide-specific antibodies, the interaction of recombinant human monoclonal IgE and Phl p 5 was studied using direct binding and blocking assays. Cross-reactivity of monoclonal IgE with group 5 allergens in several grasses was studied and inhibition experiments with patients' polyclonal IgE were performed.
resultsMonoclonal human IgE showed extensive cross-reactivity with group 5 allergens in several grasses. Despite its small size of 29 kDa, four independent epitope clusters on isoallergen Phl p 5.0101, two in each domain, were recognized by human IgE. Isoallergen Phl p 5.0201 carried two of these epitopes. Inhibition studies with allergic patients' polyclonal IgE suggest the presence of additional IgE epitopes on Phl p 5. CONCLUSIONS & CLINICAL RELEVANCE: Our results reveal the presence of a large number of independent IgE epitopes on the Phl p 5 allergen explaining the high allergenic activity of this protein and its ability to induce severe allergic symptoms. High-density IgE recognition may be a general feature of many potent allergens and form a basis for the development of improved diagnostic and therapeutic procedures in allergic disease.
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