Clinical Information

Peanut allergy is one of the most common food allergies in the United States, with an estimated prevalence of approximately 1% to 2%.(1) The clinical symptoms of peanut allergy may range from relatively mild, such as rhinorrhea, pruritus, or nausea, to a systemic and potentially life-threatening anaphylactic reaction. The diagnosis of peanut allergy is dependent upon the presence of compatible clinical symptoms in the context of peanut exposure, with support from identification of potential peanut-specific IgE allergen antibodies, either by skin testing or in vitro serology testing. In vitro testing has generally focused on assessing for the presence of total peanut IgE antibodies. These antibodies are identified by immunoassay in which the capture allergen is an extract prepared from natural peanut raw material. Most studies have demonstrated a correlation between total peanut IgE allergen antibodies and an increased likelihood of a clinical allergic response.

Once an elevated antibody response to total peanut IgE extract is established, assessment for the presence of specific IgE antibodies to the most common peanut allergenic components will be performed.

During peanut component allergen testing the presence of IgE antibodies specific for potentially allergenic individual proteins, namely Ara h 1, Ara h 2, Ara h 3, Ara h 6, Ara h 8, Ara h 9, and profilin protein Bet v2, are assessed. The determination of the relative amount of IgE antibody to specific peanut components can aid in assessment of the potential strength and type of allergenic response (see Table).

Ara h 1, 2, 3, and 6 are seed storage proteins and are the most relevant for evaluation of suspected peanut allergy.(2,3) The presence of antibodies to Ara h 2, in particular, exhibits strong association with potential systemic reactions. Ara h 1, 2, and 3-specific IgE antibodies tend to be associated with more severe allergic reactions. Ara h6 shares substantial, but not complete, cross-reactivity with Ara h2, and often exhibits similarity in terms of the degree and type of allergenicity.

Immunoglobulin E antibodies against Ara h 8 are generally associated with milder peanut allergies and may be seen in the context of birch pollen sensitization. Ara h 8 is a homologue of the birch pollen allergen Bet v1.(4) Ara h 9 is a member of the lipid transfer protein (LTP) family. LTP is ubiquitous throughout the plant kingdom and is also extremely homologous. IgE antibodies specific for Ara h 9 may be associated with allergic reactions upon peanut ingestion, although published data on this is not conclusive.(5) In addition, because of the significant sequence homology, cross-reactivity of IgE antibodies may be observed between Ara h 9 and LTP in commonly consumed plants, such as peaches, apples, and plums.

Finally, IgE antibodies to the profilin Bet v2, while associated with birch pollen sensitivity, also represent a minor peanut allergen marker as it is cross-reactive with the peanut profilin, Ara h5. As profilin proteins are present in many other foods, sensitivity to profilin Bet v2 may be associated in broad allergen cross-reactivity among foods, including mango, peach, apple, hazelnut, celery, carrot, paprika, anise, fennel, coriander, cumin, tomato, and potato. The presence of antibodies to profilin Bet v2 is typically associated with milder allergic reactions and oral allergy syndrome.

Table. Specific Peanut Allergens