Shedding Light on the Venom Proteomes of the Allergy-Relevant Hymenoptera Polistes dominula (European Paper Wasp) and Vespula spp. (Yellow Jacket).

Johannes Grosch,Christiane Hilger,Carsten B Schmidt-Weber,Antoine Lesur,Gunnar Dittmar,Markus Ollert,Stephanie Kler,Simon Blank,François Bernardin,Maria Beatrice Bilò,Maximilian Schiener

doi:10.3390/toxins12050323

Abstract

Allergic reactions to stings of Hymenoptera species can have serious or even fatal consequences. If the identification of the culprit insect is possible, venom-specific immunotherapy effectively cures Hymenoptera venom allergies. Although component-resolved diagnostics has strongly evolved in recent years, the differentiation between allergies to closely related species such as Polistes dominula and Vespula spp. is still challenging. In order to generate the basis for new diagnostic and therapeutic strategies, this study aims at resolving the venom proteomes (venomes) of these species. The venoms of P. dominula and Vespula spp. (V. germanica, V. vulgaris) were analyzed by liquid chromatography-mass spectrometry. Resulting proteins were characterized regarding their function, localization and biochemical properties. The analyses yielded 157 proteins in Vespula spp. and 100 in P. dominula venom; 48 proteins, including annotated allergens, were found in both samples. In addition to a variety of venom trace molecules, new allergen candidates such as icarapin-like protein and phospholipase A2 were identified. This study elucidates the venomes of closely related allergy-eliciting Hymenoptera species. The data indicates that relying on marker allergens to differentiate between P. dominula and Vespula spp. venom allergy is probably insufficient and that strategies using cross-reactive major allergens could be more promising.

Highlights

Allergies directed against Hymenoptera venoms are the most frequent cause of systemicIgE-mediated hypersensitivity reactions— known as anaphylaxis—in adults [1]
After removing double entries caused by similar proteins from different Hymenoptera species, After removing double entries caused by similar proteins from different Hymenoptera species, 157
The two datasets were further divided divided intodistinct three distinct groups: already annotated allergens, secreted proteins/proteinswith withknown known into three groups: already annotated allergens, secreted proteins/proteins function in the venom

Summary

Introduction

Allergies directed against Hymenoptera venoms are the most frequent cause of systemic. IgE-mediated hypersensitivity reactions— known as anaphylaxis—in adults [1]. Venom-specific immunotherapy (VIT) is currently the only known curative therapy, but its efficacy greatly depends on the correct identification of the culprit insect. In some patients a proper diagnosis is not possible despite thorough anamnesis, skin allergy tests, specific IgE (sIgE) measurement to whole venom extracts and cellular tests such as, for example, the basophil activation test (BAT). One problem-solving approach is to improve component-resolved diagnostics (CRD) by adding novel allergens to the diagnostic palette [2,3]. Various studies on insect venoms with a main focus on the order Hymenoptera yielded a variety of new allergens [4]. Discriminating venom allergy against closely related species, as for example European paper wasp (Polistes dominula) from the yellow jacket (Vespula spp.) venom allergy, remains difficult

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