Determination of the T cell epitopes of the lipocalin allergen, Rat n 1
Autor: | Paul Cullinan, Jessica Harris, Adrian Draper, Meinir Jones, A. J. Newman Taylor, H. Jeal |
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Rok vydání: | 2004 |
Předmět: |
Hypersensitivity
Immediate Allergy T-Lymphocytes Immunology Lipocalin Lymphocyte Activation Immunoglobulin E medicine.disease_cause Peripheral blood mononuclear cell Epitope Animal Technicians Epitopes Allergen immune system diseases Occupational Exposure medicine Animals Humans Immunology and Allergy Interleukin 5 Cell Proliferation Skin Tests Chi-Square Distribution integumentary system biology Laboratory animal allergy Allergens medicine.disease Rats respiratory tract diseases Occupational Diseases Cross-Sectional Studies Case-Control Studies biology.protein Interleukin-5 |
Zdroj: | Clinical Experimental Allergy. 34:1919-1925 |
ISSN: | 1365-2222 0954-7894 |
DOI: | 10.1111/j.1365-2222.2004.02126.x |
Popis: | Summary Background Laboratory animal allergy (LAA) is an important cause of occupational sensitization and asthma. Rats are a frequent cause of LAA and the major rat allergen, Rat n 1, is a member of the lipocalin protein family, which includes several other animal allergens such as the cow allergen, Bos d 2. To date, Bos d 2 is the only mammalian lipocalin allergen to have been studied in detail. Objective We undertook a cross-sectional study of a large population of individuals exposed to laboratory rats to determine the proliferative responses of peripheral blood mononuclear cells (PBMCs) to the major rat allergen, Rat n 1. Methods Eighty-three cases (defined by a positive skin prick test (SPT) 3 mm and/or a positive RAST 2% binding) and 274 referents without specific IgE to rats were tested for their proliferative responses of PBMCs to rat allergen. Cytokine release to rat urinary protein was examined in 28 sensitized and 42 non-sensitized exposed individuals. Results Proliferation to rat urinary protein was weak in all individuals. Four regions within Rat n 1 were identified as containing potential immunodominant T cell epitopes and three of these co-localized within the conserved regions of the lipocalin molecule. All four regions within Rat n 1 overlapped considerably with the characterized epitopes of the lipocalin allergen, Bos d 2. IL-5 and ratios of IL-5/IFN-γ were significantly increased in cases. Conclusion The response to Rat n 1 is remarkably similar to the cow lipocalin allergen Bos d 2. T cell epitopes within lipocalins appear to co-localize with the conserved regions of the molecule. LAA is characterized by an increased production of IL-5. Investigation of other lipocalin allergens will provide further information about the allergenicity of this group of proteins. |
Databáze: | OpenAIRE |
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