An in-silico approach of allergenicity reduction in PR10 and Profilin families of pan allergens using allergen-IgE docking analysis

Abstract

The pan-allergen includes proteins families, which are involved in general essential processes and, thus, generally distributed throughout nature. Plant pan-allergens are in charge of many IgE cross-reactions against plant food and pollen allergen sources. Pan-allergens that have been analyzed in this study are profilin and PR10 families. profilins are present in the cytoplasm of the cell and PR10 is important for controlling the growth of actin microfilaments. The cross-reactivity of IgE antibodies is a key factor in allergy occurrence. In this study, the 3-D structures of Amb a 8, Ara h 5, and Cyn d 12 of profilin family, and that of Bet v 1, Pru av 1, and Gly m 4 of PR10 family were obtained, mutated Amb a 8 (N52→S, K56→R), Ara h 5 (A54→L, A60→L), Cyn d 12 (H10→R, H19→R), Bet v 1 (N43→S, N47→S), Pru av 1 (N142→S, K152→R), Gly m 4 (K64→R, K69→R), and docked with IgE. Our results indicated that the binding energy of mutated structures to IgE decreased. This variation in the amino acid sequence and protein structure could lead to a reduction in their binding energy to IgE in the human body, resulting in a reduction in the release of histamine, which ultimately diminishes the allergy symptoms and sensitivity to the recombinant protein.