Background: No strawberry allergen has so far been identified and characterized.
Methods: Serum samples were collected from patients with a suggestive case history of adverse reactions to strawberry and other fruits. Extracts from fresh and frozen strawberries were analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), Western blotting and mass spectrometry. Patient blood samples were analysed for inhibition of IgE binding and basophil degranulation.
Results: Several IgE-binding proteins could be detected. In more than half of the patient sera, a 20/18-kDa doublet band was observed in Western blotting. These two bands were excised and analysed by mass spectrometry showing the presence of proteins belonging to the Bet v 1 family of allergens. Inhibition of the IgE binding to the 20/18-kDa doublet was obtained by addition of two recombinantly expressed allergens belonging to the Bet v 1 family (Bet v 1 and Mal d 1) and strawberry protein extract. In a cell-based assay of patient blood samples, basophil degranulation could be induced by strawberry protein extract and by Bet v 1 and Mal d 1.
Conclusions: We conclude that strawberry homologues to Bet v 1 may be allergens of importance for adverse reactions to strawberry.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1111/j.1398-9995.2004.00585.x | DOI Listing |
J Allergy Clin Immunol Pract
January 2025
Institute of Allergy, Immunology and Pediatric Pulmonology, Yitzhak Shamir Medical Center; Department of Pediatrics, Faculty of Medicine, Tel Aviv University.
Background: Data on oral immunotherapy (OIT) for hazelnut allergy is limited and its potential to cross-desensitize for other nuts is unknown.
Objective: To study the efficacy and safety of hazelnut OIT in desensitizing hazelnut and additional tree nuts.
Methods: A prospective observational study of 30 hazelnut allergic patients aged ≥4 years who underwent hazelnut OIT.
Food Res Int
January 2025
College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Jimei University, Xiamen, Fujian 361021, China; Xiamen Ocean Vocational College, Xiamen, Fujian 361100, China. Electronic address:
Food allergy incidents resulting from the consumption of Mactra quadrangularis is frequently reported. Investigating the impact of the Maillard reaction on the allergenicity of M. quadrangularis allergens is beneficial for the development of hypoallergenic mollusks aquatic products.
View Article and Find Full Text PDFJ Agric Food Chem
January 2025
State Key Laboratory of Food Science and Resources, Nanchang University, Nanchang 330047, China.
Milk proteins possess an abundance of free amino groups and exhibit diverse spatial structures. During food processing, these properties facilitate their interaction with hydrophobic ligands, such as linolenic acid. Exploring the IgE and IgG binding ability of linolenic acid-milk protein complexes at different temperatures, times, and molar ratios is crucial for controlling the allergenicity of milk proteins in food processing.
View Article and Find Full Text PDFFood Chem
December 2024
REQUIMTE-LAQV, Faculdade de Farmácia, Universidade do Porto, Rua de Jorge Viterbo Ferreira, 228, 4050-313 Porto, Portugal. Electronic address:
Edible insects are attracting increasing interest as sustainable alternative protein sources. Despite being considered a safe food for most population, their consumption can pose health risks for allergic patients. This work focused on isolating proteins from the four-European Union approved insects (Tenebrio molitor, Alphitobius diaperinus, Acheta domesticus, and Locusta migratoria) and evaluating their potential immunoglobulin E (IgE)-reactivity with crustacean-allergic patients' sera.
View Article and Find Full Text PDFJ Agric Food Chem
January 2025
School of Food Engineering, Zhangzhou Institute of Technology, Zhangzhou, Fujian 363000, China.
, a prevalent aquatic delicacy, is known to elicit allergic reactions in certain individuals. Nevertheless, the investigation into its allergenic components has remained notably inadequate. In the research, an approximately 35 kDa heat-stable protein of raw/steamed extracts was verified as tropomyosin (TM) by LC-MS/MS.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!