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Characterization of new allergens from the venom of the european paper wasp Polistes dominula.
Toxins 13:559 (2021)
Verlagsversion
Forschungsdaten
DOI
PMC
Discriminating Polistes dominula and Vespula spp. venom allergy is of growing importance worldwide, as systemic reactions to either species’ sting can lead to severe outcomes. Administering the correct allergen-specific immunotherapy is therefore a prerequisite to ensure the safety and health of venom-allergic patients. Component-resolved diagnostics of Hymenoptera venom allergy might be improved by adding additional allergens to the diagnostic allergen panel. Therefore, three potential new allergens from P. dominula venom—immune responsive protein 30 (IRP30), vascular endothelial growth factor C (VEGF C) and phospholipase A2 (PLA2)—were cloned, recombinantly produced and biochemically characterized. Sera sIgE titers of Hymenoptera venom-allergic patients were measured in vitro to assess the allergenicity and potential cross-reactivity of the venom proteins. IRP30 and VEGF C were classified as minor allergens, as sensitization rates lay around 20–40%. About 50% of P. dominula venom-allergic patients had measurable sIgE titers directed against PLA2 from P. dominula venom. Interestingly, PLA2 was unable to activate basophils of allergic patients, questioning its role in the context of clinically relevant sensitization. Although the obtained results hint to a questionable benefit of the characterized P. dominula venom proteins for improved diagnosis of venom-allergic patients, they can contribute to a deeper understanding of the molecular mechanisms of Hymenoptera venoms and to the identification of factors that determine the allergenic potential of proteins.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Allergen ; Allergen Cross-reactivity ; Hymenoptera Venom Allergy ; Phospholipase A2 ; Polistes Dominula; Soluble Forms; Hymenoptera; Recombinant; Relevant; Protein; Apis; Phospholipase-a2; Identification; Vespula; Bee
e-ISSN
2072-6651
Zeitschrift
Toxins
Quellenangaben
Band: 13,
Heft: 8,
Artikelnummer: 559
Verlag
MDPI
Verlagsort
Basel
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute for Allergy Research (IAF)
Förderungen
Helmholtz Association