Abstract
BACKGROUND: Hymenoptera venom allergy is a significant allergic reaction that affects a substantial proportion of adults. Accurate diagnosis of this allergy using venom extracts is challenging due to molecular cross-reactivity. Pure recombinant allergens offer a promising solution to identify the specific venom responsible for allergic reactions. This study aimed to produce recombinant phospholipase A5 (Ves v 5) from yellow jacket venom and evaluate the pattern of bee venom sensitization in a group of sensitive patients. METHODS AND RESULTS: A total of seven individuals, including four sensitive and three non-sensitive participants, were recruited for this study. Blood samples were collected, and serum was isolated to assess susceptibility to bee venom and recombinant allergens. Expression of Ves v 5 in Escherichia coli resulted in the production of soluble proteins, which were subsequently purified through affinity chromatography. The functionality of the recombinant allergens was evaluated through enzymatic and biophysical analyses, such as dot blot and SDS‒PAGE tests. The diagnostic relevance of Ves v 5 was further investigated using ELISA-based analyses of sera from yellow jacket venom-sensitized patients. Successful production of soluble Ves v 5 in Escherichia coli was achieved. The recombinant Ves v 5 exhibited distinct biochemical and functional characteristics. Evaluation of IgE reactivity in sera from patients underscored the importance of Ves v 5 in hymenoptera venom allergy. CONCLUSIONS: Our findings suggest that recombinant allergens can serve as an alternative to natural extracts for diagnostic purposes. Furthermore, allergen-specific immunotherapy holds the potential to enhance efficiency and specificity in the treatment of hymenoptera venom allergy.