Literature DB >> 22288514

The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of anaphylaxis and can effectively desensitize peanut-allergic mice.

M Kulis1, X Chen, J Lew, Q Wang, O P Patel, Y Zhuang, K S Murray, M W Duncan, H S Porterfield, A W Burks, S C Dreskin.   

Abstract

BACKGROUND: Ara h 2 and Ara h 6, co-purified together in a 13-25 kD fraction (Ara h 2/6; 20 kD fraction) on gel filtration chromatography, account for the majority of effector activity in a crude peanut extract (CPE) when assayed with RBL SX-38 cells sensitized with IgE from human peanut allergic sera.
OBJECTIVES: To determine if Ara h 2/6 are the primary peanut allergens responsible for allergic reactions in vivo and to determine if Ara h 2/6 would be sufficient to prevent allergic reactions to a complete CPE.
METHODS: An oral sensitization mouse model of peanut allergy was used to assess the activity of Ara h 2/6 (20 kD) and CPE without the 20 kD fraction (CPE w/o 20 kD) for allergic provocation challenge and immunotherapy. The activity of these preparations was also tested in an assay of histamine release from human basophils in whole blood.
RESULTS: Compared with mice challenged with control CPE, mice challenged with CPE w/o 20 kD experienced reduced symptoms (P < 0.05) and a smaller decrease in body temperature (P < 0.01). Results with the basophil histamine release assay corroborated these findings (P < 0.01). The mouse model was also used to administer Ara h 2/6 (20 kD) in an immunotherapy protocol, in which peanut-allergic mice treated with the 20 kD fraction experienced significantly reduced symptoms, changes in body temperature, and mast cell protease (MMCP-1) release compared with placebo (P < 0.01 for all parameters). Importantly, immunotherapy with the 20 kD fraction was just as effective as treatment with CPE, whereas CPE w/o 20 kD was significantly less effective for higher dose peanut challenges. CONCLUSIONS AND CLINICAL RELEVANCE: Ara h 2/6 are the most potent peanut allergens in vivo and can be used to desensitize peanut-allergic mice. These results have potential implications for clinical research in the areas of diagnosis and immunotherapy for peanut allergy.
© 2011 Blackwell Publishing Ltd.

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Year:  2012        PMID: 22288514      PMCID: PMC3270336          DOI: 10.1111/j.1365-2222.2011.03934.x

Source DB:  PubMed          Journal:  Clin Exp Allergy        ISSN: 0954-7894            Impact factor:   5.018


  30 in total

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4.  A murine model of peanut anaphylaxis: T- and B-cell responses to a major peanut allergen mimic human responses.

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5.  Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity.

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6.  Analysis of the effector activity of Ara h 2 and Ara h 6 by selective depletion from a crude peanut extract.

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10.  2S Albumin Storage Proteins: What Makes them Food Allergens?

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  29 in total

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3.  Human monoclonal antibodies to Ara h 2 inhibit allergen-induced, IgE-mediated cell activation.

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4.  Effect of chemical modifications on allergenic potency of peanut proteins.

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6.  Conformational IgE epitopes of peanut allergens Ara h 2 and Ara h 6.

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7.  Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut.

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9.  Ara h 2 and Ara h 6 have similar allergenic activity and are substantially redundant.

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Review 10.  Overview of component resolved diagnostics.

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