ArticleCellular and molecular life sciences : CMLS2021
Venom chemistry underlying the painful stings of velvet ants (Hymenoptera: Mutillidae).
Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Multiple mechanisms of action for an extremely painful venom.Current biology : CB · 2025Article
- Adaptive trade-offs between vertebrate defence and insect predation drive Amazonian ant venom evolution.Proceedings. Biological sciences · 2024Article
- Article
- Multiple mechanisms of action of an extremely painful venom.bioRxiv : the preprint server for biology · 2024Article
- The genome of the ant Tetramorium bicarinatum reveals a tandem organization of venom peptides genes allowing the prediction of their regulatory and evolutionary profiles.BMC genomics · 2024Article
- An Assassin's Secret: Multifunctional Cytotoxic Compounds in the Predation Venom of the Assassin BugToxins · 2023Article
- The mechanism underlying toxicity of a venom peptide against insects reveals how ants are master at disrupting membranes.iScience · 2023Article
- Article
- Profiling hymenopteran venom toxins: Protein families, structural landscape, biological activities, and pharmacological benefits.Toxicon: X · 2022Article
- Comprehensive Analysis and Biological Characterization of Venom Components from Solitary Scoliid WaspToxins · 2021Article
- Review
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Authors and funding
9 authors at 1 institution in 1 country.
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Abstract
Velvet ants (Hymenoptera: Mutillidae) are a family of solitary parasitoid wasps that are renowned for their painful stings. We explored the chemistry underlying the stings of mutillid wasps of the genus Dasymutilla Ashmead. Detailed analyses of the venom composition of five species revealed that they are composed primarily of peptides. We found that two kinds of mutillid venom peptide appear to be primarily responsible for the painful effects of envenomation. These same peptides also have defensive utility against invertebrates, since they were able to incapacitate and kill honeybees. Both act directly on cell membranes where they directly increase ion conductivity. The defensive venom peptides of Dasymutilla bear a striking similarity, in structure and mode of action, to those of the ant Myrmecia gulosa (Fabricius), suggesting either retention of ancestral toxins, or convergence driven by similar life histories and defensive selection pressures. Finally, we propose that other highly expressed Dasymutilla venom peptides may play a role in parasitisation, possible in delay or arrest of host development. This study represents the first detailed account of the composition and function of the venoms of the Mutillidae.
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