ArticlePest management science2021
Characterization of a cell death-inducing endonuclease-like venom protein from the parasitoid wasp Pteromalus puparum (Hymenoptera: Pteromalidae).
Article in Pest management science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Duplication of a conserved mitochondrial enzyme gene arms parasitoid wasps with venom cytotoxicity and oogenesis regulation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Effects of Parasitism and Venom from the EndoparasitoidInsects · 2025Article
- Article
- Oxidative, Genotoxic and Epigenotoxic Effects of Pimpla turionellae Venom at Pharmacological Perspective.Neotropical entomology · 2025Article
- A Review on Genotoxic and Genoprotective Effects of Biologically Active Compounds of Animal Origin.Toxins · 2023Review
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
backgroundParasitoid wasps are valuable natural enemies for controlling pests. To ensure successful parasitism, these wasps inject venoms along with their eggs that are deposited either into or on their hosts. Parasitoid venoms regulate host behaviors, development, metabolism and immune responses. Pteromalus puparum is a pupal endoparasitoid that parasitizes a number of butterflies, including the worldwide pest cabbage butterfly, Pieris rapae. Venom from P. puparum has a variety of effects on host hemocytes, including alteration of absolute and relative hemocyte counts, and inhibition of hemocyte spreading and encapsulation. In particular, P. puparum venom causes hemocyte cell death in vivo and in vitro.
resultsUsing assay-guided chromatography, a cell death-inducing venom fraction was identified and defined as P. puparum endonuclease-like venom protein (PpENVP). It belongs to the DNA/RNA nonspecific endonuclease family, which contains two conserved endonuclease activation sites. We analyzed its expression profiles and demonstrated that PpENVP inhibits gene expression in transfected cells relying on two activation sites. However, RNA interference of PpENVP did not significantly reduce P. puparum venom cytotoxicity, suggesting that PpENVP may not be the sole cytotoxic factor present.
conclusionOur results provide novel insight into the function of the P. puparum venom cocktail and identify a promising insecticide candidate endonuclease that targets insect hemocytes.
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