IgE binding to pepsin-digested food extracts.

Background: Pepsin resistance of allergens like lipid transfer protein and 2S albumin has been suggested as explanation for the severity of symptoms often induced by these allergens. Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characterize the risk involved in a positive in vitro IgE test. However, for many foods, purified allergens are not (yet) available.

A novel approach for the detection of potentially hazardous pepsin stable hazelnut proteins as contaminants in chocolate-based food.

Contamination of food products with pepsin resistant allergens is generally believed to be a serious threat to patients with severe food allergy. A sandwich type enzyme-linked immunosorbent assay (ELISA) was developed to measure pepsin resistant hazelnut protein in food products. Capturing and detecting rabbit antibodies were raised against pepsin-digested hazelnut and untreated hazelnut protein, respectively.

Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy.

Background: We recently described patients with soybean allergy mainly mediated by cross-reactivity to birch pollen allergens. A majority of those patients were reported to have peanut allergy.

Objective: We sought to study the occurrence of peanut allergy in patients allergic to birch pollen and characterized the Bet v 1-homologous peanut allergen Ara h 8.

In vitro and in vivo characterization of hazelnut skin prick test extracts.

Rationale: Hazelnut allergy ranks among the most frequently observed food allergies. Clinical symptoms range from the oral allergy syndrome to life threatening anaphylaxis. Diagnosis of hazelnut allergy partially relies on in vivo testing by means of skin prick testing (SPT).

How accurate and safe is the diagnosis of hazelnut allergy by means of commercial skin prick test reagents?

Background: Allergy to tree nuts, like hazelnuts, ranks among the most frequently observed food allergies. These allergies can start at early childhood and are, in contrast to other food allergies, not always outgrown by the patient. Tree nut allergy is frequently associated with severe reactions.

Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1).

Background: Serologic cross-reactivity among legumes has been described; however, it is rarely clinically significant. In this study 3 patients with a history of anaphylaxis to pea are described who subsequently had symptoms after ingestion of peanut.

Objective: We investigated whether the peanut-related symptoms were due to cross-reactivity between pea and peanut proteins.

The distribution of individual threshold doses eliciting allergic reactions in a population with peanut allergy.

Background: Hidden peanut in consumer products can endanger patients with peanut allergy. Individual threshold doses for eliciting allergic reactions need to be elucidated to assess the risks for development of allergic reactions after accidental ingestion of peanut in a population with peanut allergy.

Objective: We sought to determine the distribution of individual threshold doses in a population with peanut allergy and to correlate these thresholds to the severity of peanut-induced symptoms.

IgE to Bet v 1 and profilin: cross-reactivity patterns and clinical relevance.

Background: Individuals with pollen allergy often have IgE against plant-derived foods. This can be due to cross-reactive IgE against Bet v 1 and homologues, profilins, and/or cross-reactive carbohydrate determinants.

Objective: The aim of this study was to correlate sensitization to Bet v 1 and profilin with individual recognition patterns to plant foods and clinical relevance.