Tree nuts are considered as part of a healthy diet due to their high nutritional quality. However, they are also a potent source of allergenic proteins inducing IgE mediated hypersensitivity often causing serious, life-threatening reactions. The reported prevalence of tree nut allergy is up to 4.9% worldwide. The general term "tree nuts" comprises a number of nuts, seeds, and drupes, derived from trees from different botanical families. For hazelnut and walnut several allergens have been identified which are already partly applied in component resolved diagnosis, while for other tree nuts such as macadamia, coconut, and Brazil nut only individual allergens were identified and data on additional allergenic proteins are missing. This review summarizes the current knowledge on tree nut allergens and describes their physicochemical and immunological characterization and clinical relevance.

Cow’s milk (CM) is an integral part of our daily diet starting in infancy and continuing throughout our lifetime. Its composition is rich in proteins with a high nutritional value, bioactive components, milk minerals including calcium, and a range of immunoactive substances. However, cow’s milk can also induce a range of immune-mediated diseases including non-IgE-mediated food allergies and IgE-mediated food allergies. Cow’s milk allergens have been identified and characterized and the most relevant ones can be assigned to both, the whey and casein fraction. For preservation a range of processing methods are applied to make cow’s milk and dairy products safe for consumers. However, these methods affect milk components and thus alter the overall immunogenic activity of cow’s milk. This review summarizes the current knowledge on cow’s milk allergens and immunoactive substances and the impact of the different processes up- or downregulating the immunogenicity of the respective proteins. It highlights the gaps of knowledge of the related disease mechanisms and the still unidentified beneficial immunomodulating compounds of cow’s milk.

Walnuts are ranked high in the list of the culprit foods inducing severe allergic reactions. Jug r 2 has been identified as a major allergen in common walnut by cDNA cloning from a somatic cell line. So far, studies were performed on the allergenic activity of recombinant Jug r 2, yet there is still no evidence about the physicochemical characteristics of the natural allergen. Therefore, we aimed to purify and deeply characterize natural Jug r 2 and to assess IgE cross-reactivity among vicilins from different tree nuts. Extensive mass spectrometry analysis of the obtained purified vicilin allowed identification of the protein sequence that displayed only 44% identity to Jug r 2. The newly identified vicilin (Jug r 6) was recognized by IgE of 26% in walnut allergic patients’ sera tested. In contrast to Jug r 2, Jug r 6 displayed a remarkable level of cross-reactivity when tested with homologues from hazelnut, sesame and pistachio. It is the first report showing the necessity of proteomic studies to improve allergy component resolved diagnosis.

Summary: Background: Buckwheat (Fagopyrum esculentum) has become increasingly popular as a healthy food in Europe. However, for sensitized individuals, consumption can cause anaphylactic reactions. The aim of this study was to identify individual well‐characterized buckwheat allergens for component‐resolved diagnosis.Methods: Patients were selected by positive skin prick test to buckwheat and divided into two groups: (1) sensitized to buckwheat without clinical symptoms and (2) buckwheat allergy. Buckwheat proteins were extracted from raw buckwheat seeds, purified applying a combination of protein precipitation and chromatographic methods, and analyzed by IgE immunoblotting and ELISA.Results: Buckwheat‐allergic patients had a significantly larger median skin prick test weal diameter for buckwheat than the sensitized group and the positive control. Also, IgE immunoblotting clearly showed a distinct pattern in sera from allergic patients when compared to sensitized individuals. Several IgE‐reactive proteins were purified from crude buckwheat extract, namely legumin (Fag e 1 plus its large subunit), Fag e 2 (2S albumin), and newly identified Fag e 5 (vicilin‐like) as well as hevein‐like antimicrobial peptides, designated Fag e 4. All four allergens showed superior diagnostic precision compared to extract‐based ImmunoCAP with high sensitivity as well as high specificity.Conclusions: Patients with clinical symptoms clearly show a distinct allergen recognition pattern. We characterized a buckwheat vicilin‐like protein as a new relevant marker allergen, designated Fag e 5. Additionally, another new allergen, Fag e 4, potentially important for cross‐reactivity to latex was added to the allergen panel of buckwheat. Further, our data show that the full‐length legumin comprising both, large and small subunit should be applied for component‐resolved diagnosis. Our data indicate that concomitant sensitization to legumin, Fag e 2 and Fag e 5, predicts buckwheat allergy.