An unfolded variant of the major peanut allergen Ara h 2 with decreased anaphylactic potential.

ABSTRACT:

Background

Peanut allergy causes severe type 1 hypersensitivity reactions and conventional immunotherapy against peanut allergy is associated with a high risk of anaphylaxis.

Objective

Our current study reports proof of concept experiments on the safety of a stably denatured variant of the major peanut allergen Ara h 2 for immunotherapy. We determined the impact of structure loss of Ara h 2 on its IgE binding and basophil degranulation capacity, T cell reactivity as well as anaphylactic potential.

Methods

The secondary structure of untreated and reduced/alkylated Ara h 2 variants was determined by circular dichroism spectroscopy. We addressed human patient IgE binding to Ara h 2 by ELISA and Western blot experiments. RBL-SX38 cells were used to test the degranulation

SUBMITTER: Starkl P 

PROVIDER: S-EPMC6349134 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature