ArticleAllergy2026
Major Cat Allergen Fel d 4: Structure and Identification of a Cross-Reactive IgE-Epitope-Containing Area.
Article in Allergy, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
15 authors.
Funding
Abstract
backgroundAllergic sensitization to cats and other furry animals is a major cause of asthma and allergic rhinitis in more than 200 million people worldwide. According to the frequency of IgE recognition, allergen-specific IgE levels, and allergenic activity, Fel d 4 is a major allergen in the cat (Felis domesticus). The lipocalin allergen Fel d 4 is highly homologous to dog (Can f 6) and major horse (Equ c 1) allergens. Accordingly, IgE cross-reactivity to these allergens contributes to polysensitization and allergic responses upon exposure to different animals.
methodsFel d 4 was recombinantly produced in two systems, E. coli and Expi293F mammalian cells. Recombinant forms were characterized by circular dichroism and mass spectrometry. The Fel d 4 3D structure was determined using X-ray crystallography. Immunoreactivity, epitope analyses, and cross-reactive properties were assessed by ELISA and basophil release assays using allergic patients' sera.
resultsWe reveal the rFel d 4 crystal structures and demonstrate that mammalian cells produce an N-glycosylated recombinant Fel d 4 allergen. The C-terminal regions of Fel d 4, Can f 6, and Equ c 1 constitute conformational IgE-epitope-containing areas responsible for cross-reactivity.
conclusionUncovering the IgE-binding sites of Fel d 4 and cross-reactive allergens contributes to future rational design of active and passive allergen-specific treatment forms.
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