Background: Peanut allergy is increasing at an alarming pace in developed countries. Peanut () is a common food in Cuba. Nevertheless, reported values of sensitization and symptom severity are usually low. As our objective, we carried out an evaluation of allergic sensitivity to perform an assessment of allergic sensitization and IgE specificity profile to peanut allergens in Cuban allergic patients.
Methods: The Skin Prick Test (SPT) was performed for each patient, using two glycerinated allergenic extracts, prepared from raw or roasted peanuts. Overall, 316 food allergic patients (159 adults and 157 children) attending allergy services at four hospitals in Havana were included, as well as 303 adult non- allergic volunteers. The IgE binding profile of 26 selected SPT positive patients was further analyzed by immunoblotting.
Results: The prevalence of sensitization to peanut was 4.6% in general adult population, whereas in adult food-allergic patients it was 18.6%. Prevalence rates were even greater in food allergic children achieving 25.8%. Sensitization frequencies were apparently greater for roasted, as compared to raw peanuts, although the difference was not significant (> 0.05, Mc Nemar's). IgE binding was shown mostly by the 15 and 17 kDa bands, tentatively identified as the major allergens Ara h 2 and Ara h 6. The IgG4 binding profile was similar to IgE, although with more prominence of the bands at 37 and 28 KDa, corresponding to an Ara h 3 fragment and Peanut Agglutinin.
Discussion: The study estimated a relatively high prevalence of peanut sensitization in population. Data reported here suggest that IgE sensitization in Cuban patients is focused mostly on MW bands corresponding to the major allergens Ara h 6 and Ara h 2.
Conclusions: Sensitization to peanut allergen is indeed relatively frequent in Cuba. The IgE profile is congruent to a sensitization pattern by ingestion of roasted peanuts and is directed to well-known major allergens.
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http://dx.doi.org/10.1186/s40413-017-0156-1 | DOI Listing |
Biology (Basel)
December 2024
Graduate School of Science and Technology, Niigata University, 8050 Ikarashi 2 No-Cho, Nishi-ku, Niigata 950-2181, Japan.
Public acceptance of genetically modified crops engineered with (Bt) insecticidal protein genes (BT-GMCs), which confer resistance to various lepidopteran insect pests, is generally lacking. As a major concern over BT-GMCs is the allergenicity of insecticidal proteins, alleviating safety concerns should help increase public acceptance. In this study, three lepidopteran-specific Bt toxins, Cry1Aa, Cy1Ab, and Cry1Ac, were treated with simulated digestive fluids under various conditions.
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January 2025
College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China.
Crustaceans are delicious and highly nutritional food. However, crustaceans are one of the main food allergens, causing severe public health issues. Thus, it is important to increase the knowledge on crustacean allergens and protect the health of sensitized individuals.
View Article and Find Full Text PDFAnal Chim Acta
February 2025
Key Laboratory of Luminescence Analysis and Molecular Sensing, Ministry of Education, School of Chemistry and Chemical Engineering, Southwest University, Chongqing, 400715, PR China. Electronic address:
Background: β-lactoglobulin (β-Lg), a major allergen in dairy products, can trigger severe allergic reactions and even fatal outcomes in infants. In this work, we develop a new low background current redox recycling strategy by conjugating the electrochemical mediator to trimetallic hybrid nanoparticles (NPs)-dispersed graphene as the signal tag, which is coupled with DNAzyme amplifications to construct highly catalytic and ultrasensitive β-Lg aptasensor.
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Mol Immunol
January 2025
Department of Cell Biology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou 563003, China. Electronic address:
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January 2025
Parvalbumin is a major allergen in fish. However, there is currently no effective and safe way to remove this allergen from fish. In this study, protease gene VSP2V-280 of marine bacteria sp.
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