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• W2016995998 abstract "Summary Background Cat allergy is unique among allergy to mammals in that the major allergen Fel d 1 is a uteroglobin‐like protein and not a lipocalin. The biochemical spectrum of the cat allergens is thus uncertain, particularly with regard to the role that a cat lipocalin protein may play in sensitization to cats in allergic individuals. Objective To analyse cDNA encoding a lipocalin allergen and the corresponding recombinant allergen at both the molecular and immunological levels. Methods A submandibular salivary gland cDNA expression library was constructed and screened for clones producing IgE‐binding polypeptides. cDNA encoding a lipocalin allergen and its corresponding recombinant allergen were analysed. Results An IgE binding molecule with high sequence identity to the boar salivary lipocalin and the horse lipocalin Equ c 1 allergen was isolated and designated, Fel d 4. Serum from 62.96% of cat‐allergic subjects examined had measurable IgE antibody to Fel d 4 but typically at low levels. Despite this in 47% of sera the anti‐Fel d 4 IgE titres were higher than the anti‐Fel d 1 titres. IgE binding to the lipocalin allergen could be blocked by an allergen extract from cow and to a lesser degree by extracts from horse and dog. Conclusion Fel d 4 is a lipocalin allergen produced by the cat, which binds IgE at relatively high frequency in cat‐sensitive individuals. The allergen provides not only a means for investigating differences in the immune response to lipocalin allergens from that found for other mammalian species but also an important reagent for the diagnosis of cat allergy." @default.
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• W2016995998 date "2004-11-01" @default.
• W2016995998 modified "2023-10-14" @default.
• W2016995998 title "Fel d 4, a cat lipocalin allergen" @default.
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• W2016995998 doi "https://doi.org/10.1111/j.1365-2222.2004.02090.x" @default.
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