Abstract
The aim of this study was to purify potential allergenic components of Vespa velutina venom, the yellow legged Asian Hornet, and perform a preliminary characterization of the purified proteins. Starting from the whole venom of V.velutina, several chromatographic steps allowed to purify the phospholipase (named Vesp v 1), as well as the antigen 5 (Vesp v 5, the only allergenic component described as such so far). The two hyaluronidase isoforms found (Vesp v 2A and Vesp v 2B) cannot be separated from each other, but they are partially purified and characterized. Purity of the isolated proteins in shown by SDSPAGE, as well as by the results of the N-terminal sequencing. This characterization and nLC-MS/MS data provide most of the sequence for Vesp v 1 and Vesp v 5 (72 and 84% coverage, respectively), confirming that the whole sequences of the isolated natural components match with the data available in public transcriptomic databases. It is of particular interest that Vesp v 1 is a glycosylated phospholipase, a fact that had only described so far for the corresponding allergen components of Dolichovespula maculata and Solenopsis invicta. The availability of the complete sequences of Vespa velutina components permits comparison with homologous sequences from other Hymenoptera. These data demonstrate the higher similarity among the species of the genera Vespa and Vespula, in comparison to Polistes species, as it is especially observed with the hyaluronidases isoforms: the isoform Vesp v 2A only exists in the former genera, and not in Polistes; in addition, the most abundant isoform (Vesp v 2B) exhibits 93% sequence identity with the Ves v 2 isoform of Vespula vulgaris. Finally, the isolated components might be useful for improving the diagnosis of patients that could be allergic to stings of this invasive Asian hornet, as it has been the case of an improved diagnosis and treatment of other Hymenoptera-sensitized patients.
Highlights
The “yellow-legged”-Asian hornet (Vespa velutina nigrithorax) is an invasive species that was originally introduced in the Iberian Peninsula through France, having been identified in Spain
The complete sequences for Vesp v 5, Vesp v 1, Vesp v 2A and Vesp v 2B data can be accessed from the UniProt Knowledgebase with the following accession numbers: P0DMB9 for Vesp v 5, C0HLL3 for Vesp v 1, C0HLL4 for hyaluronidase A (Vesp v 2A) and C0HLL5 for hyaluronidase B (Vesp v 2B)
The relevant natural venom components (A1 phospholipase, antigen 5 and hyaluronidases) were purified from lyophilized Vespa velutina venom sac extract of individual hornets collected in Europe (ALK Source Materials Inc., Spring Mills, U.S.A.; batch 01071301AH)
Summary
The “yellow-legged”-Asian hornet (Vespa velutina nigrithorax) is an invasive species that was originally introduced in the Iberian Peninsula through France, having been identified in Spain. Purification of Vespa velutina venom components the proteins). The protocols followed in this manuscript are explained in the Materials and Methods section, as well as with the corresponding citations of the manuscripts that first performed the corresponding studies for, e.g. purification, enzymatic activity measurement, etc. The data from our experimental determinations have been deposited in public repositories and are freely accessible. The LTQ Orbitrap Velos raw files and files with data of all the peptides identified for the purified Vesp v 5 and Vesp v 1 are freely accessible and are indexed as ProteomeXchange dataset PXD015381 and included in the MassIVE server. The complete sequences for Vesp v 5, Vesp v 1, Vesp v 2A and Vesp v 2B data can be accessed from the UniProt Knowledgebase with the following accession numbers: P0DMB9 for Vesp v 5, C0HLL3 for Vesp v 1, C0HLL4 for hyaluronidase A (Vesp v 2A) and C0HLL5 for hyaluronidase B (Vesp v 2B)
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