About 50–70% of patients allergic to birch pollen suffer from sensitization after apple ingestion. Apple allergenicity was established in only few varieties. Studies were performed on apple fruits of 21 traditional and nine modern varieties organically, intensively, or integratively produced. The aim of the study was to assess whether the factors like cultivation method, maturity stage, genotype, or type of tissue place an impact on the allergenic potential of apples. To answer these questions, we used semiquantitative real-time PCR, ELISA, and immunoblotting. Apple allergen genes present divergent expression across apple cultivars. Expression of the Mal d 1.06A correlates with the Mal d 1 level and is affected by the cultivation method and maturity of the fruit. The content of the main allergen Mal d 1 varied widely across cultivars. Interestingly, in our study, the Gala variety presented a low Mal d 1 concentration regardless of the cultivation method. Based on the Mal d 1.06A expression, the Mal d 1 protein content, and the immunoreactivity assay, the Kandil Sinap, Kosztela, Rumianka from Alma-Ata, Kantówka Gdańska, Reinette Coulon, and Gala cultivars emerged as potentially hypoallergenic apple cultivars. Our study allowed distinguishing between potentially low, medium, and highly allergenic varieties.

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Due to the observed increase of consumption of lupine-fortified food products and the high homology of lupine protein to other legumes, occurrence of new lupine allergy cases can increase significantly. Therefore, the aim of this study was to compare the seeds of 18 new Polish lupine breeding lines for immunoreactivity in relation to the sera of the patients sensitized to cross-reacting allergens, i.e. to soybeans and peanuts, using the western blot method. Antibodies present in the sera obtained from two adult outpatients cross-reacted with the studied extracts and made it possible to indicate six lines with decreased expression of Lup an 1 (high molecular weight subunit of β-conglutin): Mandelup, Mirela, Puławski Różowy Wczesny, Ignis, 25-65-M-4-1 and Stadoliszczenskij L-610 lines. Two more lines (Schmalblaettrige Schwerzplatzen and Rammiespielyj) are probably also less immunoreactive, due to the decreased content of alkaline subunit of α-conglutin-Lup an 2. The highest variability in immunoreactivity of proteins in question was noted for peptides with molecular weights ~ 20, 23, 28, 33, 38, 39, 43, 49, 50 and 63 kDa. Unfortunately, different patterns of immunoreactivity of the seeds obtained from various cultivation sites was noted for some lines. The correlation between the total protein content and reduced immunoreactivity of the tested lines was not confirmed. Thus, the lines with decreased immunoreactivity could be considered material for future crossing the narrow-leafed lupine lines to obtain varieties intended for food production.

Background. Small amounts of protein can be found in honey, including well known allergen sources, such as plant pollen and honeybee secretions. Despite this, there are few case reports describing allergic reactions following the consumption of honey. The aim of this study was to examine the allergenic properties of nectar honey collected throughout the entire beekeeping season from different provinces in Poland. Materials and methods. The immunoreactive properties of 20 Polish nectar honeys were analysed using the sera of IgE pollen allergenic patients (n = 5). The botanical origins and pollen of the anemophilous plants in the studied honeys were identified through palynological analysis. Results. The significant differences in the protein content between the five varieties of honey and the differences in protein pattern and pollen profiles were observed. All of the honey samples contained immunoreactive fractions reacting with IgE present in the sera of patients allergenic to different pollens. Conclusions. Although honey allergies are reported relatively rarely, all the tested samples of Polish nectar honeys contained many protein fractions which reacted with the IgE antibodies of allergenic patients. In all samples, the immunoreactive protein band with a molecular weight around 60 kDa, probably secreted by bees, was present. The results do not allow the immunoreactive fractions characteristic for particular honey varieties to be identified.

The results of the study can contribute to identification of yet undetected allergens of narrow-leafed lupin. This, in turn, can make lupin-fortified products safer for the consumers.