Premium
Allergenic characteristics of a modified peanut allergen
Author(s) -
King Nina,
Helm Ricki,
Stanley J. Steven,
Vieths Stefan,
Lüttkopf Dirk,
Hatahet Lina,
Sampson Hugh,
Pons Laurent,
Burks Wesley,
Ban Gary A.
Publication year - 2005
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200500073
Subject(s) - allergen , epitope , immunoglobulin e , degranulation , desensitization (medicine) , immunology , allergy , chemistry , anaphylaxis , peanut allergy , microbiology and biotechnology , biology , antibody , biochemistry , receptor
Attempts to treat peanut allergy using traditional methods of allergen desensitization are accompanied by a high risk of anaphylaxis. The aim of this study was to determine if modifications to the IgE‐binding epitopes of a major peanut allergen would result in a safer immunotherapeutic agent for the treatment of peanut‐allergic patients. IgE‐binding epitopes on the Ara h 2 allergen were modified, and modified Ara h 2 (mAra h 2) protein was produced. Wild‐type (wAra h 2) and mAra h 2 proteins were analyzed for their ability to interact with T‐cells, their ability to bind IgE, and their ability to release mediators from a passively sensitized RBL‐2H3 cell line. Multiple T‐cell epitopes were identified on the major peanut allergen, Ara h 2. Ara h 2 amino acid regions 11–35, 86–125, and 121–155 contained the majority of peptides that interact with T‐cells from most patients. The wAra h 2 and mAra h 2 proteins stimulated proliferation of T‐cells from peanut‐allergic patients to similar levels. In contrast, the mAra h 2 protein exhibited greatly reduced IgE‐binding capacity compared to the wild‐type allergen. In addition, the modified allergen released significantly lower amounts of β‐hexosaminidase, a marker for IgE‐mediated RBL‐2H3 degranulation, compared to the wild‐type allergen.