期刊
MOLECULAR IMMUNOLOGY
卷 48, 期 4, 页码 637-646出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2010.11.001
关键词
Fish; Parvalbumin; Allergic asthma; Occupational asthma; Food allergy; Mouse
资金
- South African Research Chair initiative of the Department of Science and Technology
- National Research Foundation (NRF)
- University of Cape Town
- Medical Research Council
- National Research Foundation (NRF) of South Africa
- Royal Society U.K.
- GlaxoSmithKlein/ALLSA
- Wellcome Trust [056708/Z/99]
- Christian Doppler Association [F01804]
- Biomay (Vienna, Austria)
Aerosolized fish proteins are an important cause of allergic airway reactions in both the domestic and the occupational environment. The aim of this study was to investigate inhalant fish-induced allergy in a mouse model and compare immune responses generated by raw and heat-treated fish extracts as well as natural and recombinant forms of the major fish allergen parvalbumin. Mice were sensitized with raw or cooked pilchard extract and challenged intranasally with cooked pilchard extract, purified natural pilchard parvalbumin or recombinant carp parvalbumin (rCyp c1.01). Cooked pilchard extract predominantly sensitized mice to parvalbumin and induced specific IgG1 and IgE antibodies against both pilchard parvalbumin and rCyp c1.01, whereas additional allergens were recognized by mice sensitized with raw extract, including a 36 kDa allergen that was also recognized by fish processing workers and was identified as glyceraldehyde-3-phosphate dehydrogenase. Mice challenged with cooked extract and purified pilchard parvalbumin had increased Th2 cytokine production in mediastinal lymph node cells and splenocytes, whereas mice challenged with rCypc1.01 did not. This study identifies a new IgE-binding protein that may be important in occupational allergy to fish and demonstrates the feasibility of testing recombinant allergens for immunotherapeutic potential in vivo. (C) 2010 Elsevier Ltd. All rights reserved.
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