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.
Highlights
Strawberries are one of the most economically important fruit crops and are highly appreciated worldwide due to their delicate taste and aroma, as well as for their beneficial effects on human health
Since Fra a 1.02 is the most expressed allergen in the ripe strawberry fruit and has been identified as highly allergenic,[5,9,16] it is considered as the main responsible allergen causing type I pollen-related allergies to strawberry
The structural analysis of Fra a 1.02 could contribute to elucidate the residues involved in IgE binding and help generate strategies to eliminate or minimize the allergenic potential of the fruits
Summary
Strawberries are one of the most economically important fruit crops and are highly appreciated worldwide due to their delicate taste and aroma, as well as for their beneficial effects on human health.
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