ArticleInfection and immunity1999
Conformational and linear B-cell epitopes of Asp f 2, a major allergen of Aspergillus fumigatus, bind differently to immunoglobulin E antibody in the sera of allergic bronchopulmonary aspergillosis patients.
Article in Infection and immunity, 1999. 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, 54 citations in OpenAlex.
- Serological and biochemical characterization of Aspergillus fumigatus Asp f 10 as a potential diagnostic marker in ABPA and related respiratory diseases.Frontiers in allergy · 2026Article
- Identification of immunodominant IgE epitopes of the major house dust mite allergen Der f 24.International journal of molecular medicine · 2019Article
- Epitope Mapping of Rhi o 1 and Generation of a Hypoallergenic Variant: A CANDIDATE MOLECULE FOR FUNGAL ALLERGY VACCINES.The Journal of biological chemistry · 2016Article
- Mold allergens in respiratory allergy: from structure to therapy.Allergy, asthma & immunology research · 2015Review
- Fungal allergens.Current allergy and asthma reports · 2003Review
- Identification of continuous B-cell epitopes on the protein moiety of the 58-kiloDalton cell wall mannoprotein of Candida albicans belonging to a family of immunodominant fungal antigens.Infection and immunity · 2001Article
- Molecular biology and immunology of fungal allergens.Indian journal of clinical biochemistry : IJCB · 2000Article
- Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies.The Biochemical journal · 2000Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Asp f 2 is a major Aspergillus fumigatus allergen involved in allergic bronchopulmonary aspergillosis. Knowledge of the B-cell epitopes may contribute to the understanding of immunoregulation and immunodiagnosis. To elucidate the immunoglobulin E (IgE) binding epitopes in the linear sequence of Asp f 2, we synthesized decamer peptides spanning the whole molecule of Asp f 2 on derivatized cellulose membranes and evaluated IgE binding in ABPA patient and control sera. Peptides three to five amino acids long were synthesized based on amino acid sequences within the IgE binding regions and evaluated for the specificity of epitope antibody interactions. Nine IgE binding regions were recognized in this protein of 268 amino acid residues. Of the nine epitopes, seven (ATQRRQI, RKYFG, HWR, YTTRR, DHFAD, ALEAYA, and THEGGQ) are present in the hydrophilic regions of Asp f 2. Immunologic evaluation of the three recombinant fragments, Asp f 2A encompassing the N-terminal epitope region, Asp f 2B without N- and C-terminal regions of the protein, and Asp f 2C representing C-terminal epitopes, revealed that either the N- or C-terminal region of the protein is essential for the correct folding and conformation for IgE antibody binding.
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