Proteome and Allergenome of Asian Wasp, Vespa affinis, Venom and IgE Reactivity of the Venom Components

Abstract

Vespa affinis (Asian wasp, Thai banded tiger wasp, or local name: Tor Hua Seua) causes the most frequent incidence of medically important Hymenoptera sting in South and Southeast Asia. However, data on the venom components attributable to the sting derived-clinical manifestations (local reactions, IgE mediated-anaphylaxis, or systemic envenomation) are lacking. This study provides the first set information on V. affinis venom proteome, allergenome, and IgE reactivity of individual venom components. From 2DE-gel based-proteomics, the venom revealed 93 protein spots, of which proteins in 51 spots could be identified and classified into three groups: typical venom components and structural and housekeeping proteins. Venom proteins in 32 spots reacted with serum IgE of wasp allergic patients. Major allergenic proteins that reacted to IgE of >50% of the wasp allergic patients included PLA1 (100%), arginine kinase (73%), heat shock 70 kDa protein (73.3%), venom allergen-5 (66.7%), enolase (66.7%), PLA1 magnifin (60%), glyceraldehyde-3-phosphate dehydrogenase (60%), hyaluronidase (53.3%), and fructose-bisphosphate aldolase (53.3%). The venom minor allergens were GB17876 transcript (40%), GB17291 transcript (20%), malic enzyme (13.3%), aconitate hydratase (6.7%), and phosphoglucomutase (6.7%). The information has diagnostic and clinical implications for future improvement of case diagnostic sensitivity and specificity, component-resolve diagnosis, and design of specific Hymenoptera venom immunotherapy.

Comparative proteomic analysis of two wasps venom, Vespa tropica and Vespa affinis

“…Their nests are generally elongated, similarly to the nests of Vespa velutina ( Fig. 1C; (Lee et al, 2005;Sookrung et al, 2014)). VT is a subterranean species.…”

Towards complete identification of allergens in Jack Jumper (Myrmecia pilosula) ant venom and their clinical relevance: An immunoproteomic approach

“…AK is a 40 kDa enzyme that is involved in energy metabolism in invertebrates . AK has been reported as a cross‐reactive pan‐allergen found in several invertebrate species, including in honeybee and wasps . Similar to the venom of the social wasp Polybia paulista , the AK present in JJAV was also glycosylated.…”

Current challenges in molecular diagnostics of insect venom allergy

“…Interestingly, few studies for whole venome and allergome profiling of European Vespinae and Polistinae species are currently available, hampering the identification of novel allergens which can be used as potential subfamily-specific biomarkers. Previous systemic analysis from venome profiling of the Neotropical paper wasp [37] and the Asian hornet Vespa affinis [38] resulted in the detection of several novel proteins which were recognized by IgE in the sera of sensitized patients. Unfortunately, the potential role of these proteins as relevant allergens remains largely unexplored.…”