Venom chemistry underlying the painful stings of velvet ants (Hymenoptera: Mutillidae)

Cell Mol Life Sci. 2021 Jun;78(12):5163-5177. doi: 10.1007/s00018-021-03847-1. Epub 2021 May 10.

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.

Keywords: Cow killer; Dasymutilla; Pain; Parasitoid; Wasp.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Venoms / chemistry*
  • Arthropod Venoms / toxicity*
  • Behavior, Animal / drug effects*
  • Female
  • Hymenoptera / physiology*
  • Insect Bites and Stings / chemically induced*
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Pain / chemically induced*
  • Peptide Fragments / toxicity*
  • Sequence Homology

Substances

  • Arthropod Venoms
  • Peptide Fragments