ArticleJournal of agricultural and food chemistry2020
Structural Bases for the Allergenicity of Fra a 1.02 in Strawberry Fruits.
Article in Journal of agricultural and food chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- A systematic review of allergen cross-reactivity: Translating basic concepts into clinical relevance.The journal of allergy and clinical immunology. Global · 2024Review
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- Sensitizations to wheat and strawberry: are they a tangible threat to atopic Egyptian.American journal of clinical and experimental immunology · 2022Article
- Structure and Zeatin Binding of the Peach AllergenJournal of agricultural and food chemistry · 2021Article
- Down-regulation of Fra a 1.02 in strawberry fruits causes transcriptomic and metabolic changes compatible with an altered defense response.Horticulture research · 2021Article
- Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
Abstract
Although strawberries are highly appreciated fruits, their intake can induce allergic reactions in atopic patients. These reactions can be due to the patient's previous sensitization to the major birch pollen allergen Bet v 1, by which IgE generated in response to Bet v 1 cross-reacts with the structurally related strawberry Fra a 1 protein family. Fra a 1.02 is the most expressed paralog in ripe strawberries and is highly allergenic. To better understand the molecular mechanisms regulating this allergic response, we have determined the three-dimensional structure of Fra a 1.02 and four site-directed mutants that were designed based on their positions in potential epitopes. Fra a 1.02 and mutants conform to the START fold. We show that the cross-reactivity of all the mutant variants to IgE from patients allergic to Bet v 1 was significantly reduced without altering the conserved structural fold, so that they could potentially be used as hypoallergenic Fra a 1 variants for the generation of vaccines against strawberry allergy in atopic patients.
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Registered trials
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