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Flow Cytometric Analysis of Particle-bound Bet v 1 Allergen in PM10
Published on: November 19, 2016
Insights into structural and binding studies of pollen allergen Bet v 1 using computational approaches
Mansi Pandit1, Nandita Narayanasamy2, N Latha1
1Bioinformatics Infrastructure Facility, Sri Venkateswara College (University of Delhi), Benito Juarez Road, Dhaula Kuan, New Delhi, 110021 India.
None:
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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