ArticleScientific reports2017
Clustering of conformational IgE epitopes on the major dog allergen Can f 1.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Human IgE monoclonal antibodies define two unusual epitopes trapping dog allergen Can f 1 in different conformations.Protein science : a publication of the Protein Society · 2025Article
- Furry Animal Allergy: Lipocalins, Serum Albumins, and Secretoglobins-Cross-Reactivity, Diagnosis, and Management Strategies.Clinical reviews in allergy & immunology · 2025Review
- Impact of Semiochemicals Binding to Fel d 1 on Its 3D Conformation and Predicted B-Cell Epitopes Using Computational Approaches.International journal of molecular sciences · 2023Article
- Human Monoclonal IgE Antibodies-a Major Milestone in Allergy.Current allergy and asthma reports · 2023Review
- IgE Epitopes of the House Dust Mite Allergen Der p 7 Are Mainly Discontinuous and Conformational.Frontiers in immunology · 2021Article
- Immune-related genes play an important role in the prognosis of patients with testicular germ cell tumor.Annals of translational medicine · 2020Article
- Structural Aspects of the Allergen-Antibody Interaction.Frontiers in immunology · 2020Review
- Ole e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE response in olive pollen allergic patients.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Immunoglobulin E (IgE)-associated allergy affects more than 25% of the population. Can f 1 is the major dog allergen associated with respiratory symptoms but the epitopes recognized by allergic patients IgE on Can f 1 are unknown. To characterize IgE epitopes of Can f 1 recognized by dog allergic patients, six overlapping peptides spanning the Can f 1 sequence were synthesized. In direct IgE epitope mapping experiments peptides were analyzed for IgE reactivity by dot blot and Enzyme-linked immunosorbent assay (ELISA) with sera from dog allergic patients. For indirect epitope-mapping, rabbits were immunized with the peptides to generate specific IgG antibodies which were used to inhibit allergic patients' IgE binding to Can f 1. IgE binding sites were visualized on a model of the Can f 1 three-dimensional structure. We found that Can f 1 does not contain any relevant sequential IgE epitopes. However, IgE inhibition experiments with anti-peptide specific IgGs showed that Can f 1 N- and C-terminal portion assembled a major conformational binding site. In conclusion, our study is the first to identify the major IgE epitope-containing area of the dog allergen Can f 1. This finding is important for the development of allergen-specific treatment strategies.
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Registered trials
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