mediator release assays were performed and IgE cross-reactivity was evaluated by ELISA and Immuno Solid-phase Allergen Chip (ISAC) IgE inhibition assays.ResultsAll allergens showed the typical Bet v 1-like secondary structure elements, and they were all able to bind serum IgE from Fagales allergic...
Secretome analysis of chickpea reveals dynamic extracellular remodeling and identifies a Bet v1-like protein, CaRRP1 that participates in stress response. Sci. Rep. 5, 18427 (2015).Gupta, S.; Wardhan, V.; Kumar, A.; Rathi, D.; Pandey, A.; Chakraborty, S.; Chakraborty, N. Secretome ...
Here, we give structural evidence that Bet v 1 is a lipocalin-like protein with a striking structural resemblance to human lipocalin 2. Lipocalin 2 is highly expressed in the lung where it exerts immunoregulatory functions dependent on being loaded with siderophore-bound iron (holo-form) or ...
The enzyme is a dimer and exhibits a Bet v1-like fold. The Bet v1 superfamily is composed of sequences related to the major Birch (Betula verrucose) pollen allergen Bet v1. The fold is composed of an anti-parallel β-sheet, which is wrapped around a long C-terminal α-helix (Fig...
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Here, we give structural evidence that Bet v 1 is a lipocalin-like protein with a striking structural resemblance to human lipocalin 2. Lipocalin 2 is highly expressed in the lung where it exerts immunoregulatory functions dependent on being loaded with siderophore-bound iron (holo-form) or not...
The ubiquitous taxonomic distribution of Bet v 1-like superfamily members and their ligand binding activities suggest that the Bet v 1 fold can be traced back to the last universal common ancestor and that the primordial Bet v 1-like protein probably functioned as a lipid carrier....
The enzyme is a dimer and exhibits a Bet v1-like fold. The Bet v1 superfamily is composed of sequences related to the major Birch (Betula verrucose) pollen allergen Bet v1. The fold is composed of an anti-parallel β- sheet, which is wrapped around a long C-terminal α-...