Current Understanding of Cross‐Reactivity of Food Allergens and Pollen

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Abstract
Abstract: Pollen‐allergic patients frequently present allergic symptoms after ingestion of several kinds of plant‐derived foods. The majority of these reactions is caused by four distinct cross‐reactive structures that are present in birch pollen. Proteins that share common epitopes with Bet v 1, the major birch pollen allergen, occur in pollens of several tree species: apples, stone fruits, celery, carrot, nuts, and soybeans. Approximately 70% of our patients who are allergic to birch pollen may experience symptoms after consumption of foods from these groups. In contrast, two minor allergenic structures—profilins and cross‐reactive carbohydrate determinants (CCD)—that sensitize approximately 10‐20% of all pollen‐allergic patients are also present in grass pollen and weed pollen. Moreover, IgE‐binding proteins related to the birch pollen minor allergen Bet v 6 have been found in many vegetable foods such as apple, peach, orange, lychee fruit, strawberry, persimmon, zucchini, and carrot. Frequently, the occurrence of cross‐reactive IgE antibodies is not correlated with the development of clinical food allergy. In particular, the clinical relevance of sensitization to CCD is doubtful. Generally, pollen‐related allergens tend to be more labile during heating procedures and in the digestive tract compared to allergens from classical allergenic foods such as peanut. However, recent DBPCFC studies have shown that both cooked celery and roasted hazelnuts still pose an allergenic risk for pollen‐sensitized subjects. Since pathogenesis‐related proteins share several common features with allergens and both the Bet v 1 and the Bet v 6‐related food allergens are defense‐related proteins, approaches to introduce such proteins as a measure to protect plants against diseases should be performed with caution as they may increase the allergenicity of these crops.