ArticleIn silico pharmacology2025
Insights into structural and binding studies of pollen allergen Bet v 1 using computational approaches.
Article in In silico pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Bet v 1, the European White Birch tree pollen allergen is responsible for a number of allergic responses in humans such as rhinitis, asthma and oral allergy syndrome. The allergen belongs to pathogenesis-related (PR) class 10 protein superfamily and exists in several naturally occurring isoforms. Limited structural information on Bet v 1 isoallergens and variants prompted us to carry out their in silico structural characterization. In this study, three-dimensional structures of Bet v 1 isoallergens were predicted followed by allergen-antibody docking with Bet v 1- specific human IgE. Further, molecular dynamics simulations were performed for the allergen-antibody complexes. In addition, in silico mutagenesis was carried out for the design of a hypoallergenic variant of Bet v 1. Our study aimed to elucidate the differential ability of Bet v 1 isoallergens in eliciting allergic responses based on structural features and also identified a potential hypoallergen allowing us to propose it as a promising candidate for treating birch pollen-induced allergy. Supplementary Information: The online version contains supplementary material available at 10.1007/s40203-024-00303-3.
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