ArticlePloS one2020
Purification and molecular characterization of phospholipase, antigen 5 and hyaluronidases from the venom of the Asian hornet (Vespa velutina).
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Integrated Venomics Profiling of Apis dorsata and Vespa sp. Venoms Reveal Putative Bioactive Candidates.Chemistry & biodiversity · 2026Article
- Biomarkers for the Molecular Diagnosis of IgE-Mediated Hymenoptera Venom Allergy in Clinical Practice.International journal of molecular sciences · 2024Review
- Article
- A deeper insight into the sialome of male and female Culex quinquefasciatus mosquitoes.BMC genomics · 2023Article
- A deeper insight into the sialome of male and female Ochlerotatus triseriatus mosquitoes.Insect biochemistry and molecular biology · 2022Article
- Bioactive Peptides and Proteins from Wasp Venoms.Biomolecules · 2022Review
- Integrated analysis of the sialotranscriptome and sialoproteome of the rat flea Xenopsylla cheopis.Journal of proteomics · 2022Article
- Review
- Overview of protein posttranslational modifications in Arthropoda venoms.The journal of venomous animals and toxins including tropical diseases · 2022Review
- Asian Hornet,Molecules (Basel, Switzerland) · 2021Article
- Newly defined allergens in the WHO/IUIS Allergen Nomenclature Database during 01/2019-03/2021.Allergy · 2021Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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