The high molecular weight dipeptidyl peptidase IV Pol d 3 is a major allergen of Polistes dominula venom

Abstract

Hymenoptera venom allergy can cause severe anaphylaxis in untreated patients. Polistes dominula is an important elicitor of venom allergy in Southern Europe as well as in the United States. Due to its increased spreading to more moderate climate zones, Polistes venom allergy is likely to gain importance also in these areas. So far, only few allergens of Polistes dominula venom were identified as basis for component-resolved diagnostics. Therefore, this study aimed to broaden the available panel of important Polistes venom allergens. The 100 kDa allergen Pol d 3 was identified by mass spectrometry and found to be a dipeptidyl peptidase IV. Recombinantly produced Pol d 3 exhibited sIgE-reactivity with approximately 66% of Polistes venom-sensitized patients. Moreover, its clinical relevance was supported by the potent activation of basophils from allergic patients. Cross-reactivity with the dipeptidyl peptidases IV from honeybee and yellow jacket venom suggests the presence of exclusive as well as conserved IgE epitopes. The obtained data suggest a pivotal role of Pol d 3 as sensitizing component of Polistes venom, thus supporting its status as a major allergen of clinical relevance. Therefore, Pol d 3 might become a key element for proper diagnosis of Polistes venom allergy.

CAP-Inhibition, Molecular Diagnostics, and Total IgE in the Evaluation of <b><i>Polistes</i></b> and <b><i>Vespula</i></b> Double Sensitization

“…The most common vespid stings leading to anaphylactic reactions involve the Polistes dominula (PD) and Ves­pula ( VV) species in southern Europe, and cross-reactions between them are well documented [1-3]. However, current routinely performed in vitro and in vivo diagnostics are not able to clinically distinguish between irrelevant cross-reactivity and real double sensitization to vespid venom.…”

“…1). Molecular allergy research and development will likely help in sequencing new species-specific antigens for vespids, especially PD, whose antigen 1 (phospholipase) is not currently available for routinely diagnostic use; this would markedly increase the accuracy, making a Ves v 1/Pol d 1 comparison possible [1]. For the time being, the recombinant allergens currently in use, i.e., Ves v 5, Pol d 5, and Ves v 1, do not provide sufficient accuracy.…”

“…The Ves v 5/tIgE and Pol d 5/tIgE ratios seem to be more accurate when compared to Ves v 5 or Pol d 5 sIgE values alone, and to the Ves v 5/Pol d 5 (or vice versa) ratio. Furthermore, according to very recent studies, other major allergens may play a pivotal role in the diagnosis of PD allergic patients [1]. …”

From basic science to diagnostics ‐ History of a patent on a honeybee venom allergen

“…Its putative function in HBV is the processing and activation of the membrane‐toxic peptide melittin. The role of Api m 5 as major allergen of HBV was confirmed by its pronounced sIgE reactivity and the potent activation of basophils from HBV‐allergic patients …”

“…Subsequently, the Api m 5 homologues from Vespula vulgaris and Polistes dominula venom Ves v 3 and Pol d 3 were identified and characterized . Due to the extent of homology, both major allergens are protected by the same patent.…”