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

• Published in: Toxins Vol. 12; no. 5; p. 323
• Main Authors: Grosch, Johannes, Hilger, Christiane, Bilò, Maria Beatrice, Kler, Stephanie, Schiener, Maximilian, Dittmar, Gunnar, Bernardin, François, Lesur, Antoine, Ollert, Markus, Schmidt-Weber, Carsten B, Blank, Simon
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 14-05-2020; MDPI
• Subjects: allergen; Allergens; Allergens - analysis; Allergens - immunology; Allergic reactions; Allergies; Animals; Annotations; Antigens; Arthropod Venoms - chemistry; Arthropod Venoms - immunology; Bees; Chromatography, Liquid; Cures; Diagnostic systems; European paper wasp; Extracellular matrix; Hymenoptera; Hymenoptera - classification; Hymenoptera - immunology; Hymenoptera - metabolism; Hymenoptera venom allergy; Hypersensitivity - diagnosis; Hypersensitivity - immunology; Hypersensitivity - therapy; Immunotherapy; Insect Bites and Stings - diagnosis; Insect Bites and Stings - immunology; Insect Bites and Stings - therapy; Insect Proteins - analysis; Insect Proteins - immunology; Insects; Liquid chromatography; Localization; Mass spectrometry; Mass spectroscopy; Molecular weight; Phospholipase; Phospholipase A2; Polistes dominula; Polistes dominula venom; Polypeptides; Proteins; Proteome; Proteomics; Species; Stings; Tandem Mass Spectrometry; Venom; venom proteome; Vespula; Vespula spp. venom; allergen; European paper wasp; Vespula spp. venom; venom proteome; yellow jacket; Polistes dominula venom; Hymenoptera venom allergy
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins12050323

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
and
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
and
spp. (
,
) were analyzed by liquid chromatography-mass spectrometry. Resulting proteins were characterized regarding their function, localization and biochemical properties. The analyses yielded 157 proteins in
spp. and 100 in
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
and
spp. venom allergy is probably insufficient and that strategies using cross-reactive major allergens could be more promising.