Proteomic Analysis of the Venom from the Ruby Ant and the Isolation of a Novel Insecticidal Decapeptide.

Ants are a biodiverse group of insects that have evolved toxic venom containing many undiscovered bioactive molecules. In this study, we found that the venom of the ruby ant is a rich source of peptides. LC-MS analysis revealed the presence of 142 different peptides varying in molecular weight, sequence length, and hydrophobicity. One of the most abundant peaks was selected for further biochemical and functional characterization. Combined Edman degradation and de novo peptide sequencing revealed the presence of a novel decapeptide (myrmicitoxin) with the amino acid sequence NH₂-IDPKLLESLA-CONH₂. The decapeptide was named U-MYRTX-MRArub1 and verified against a synthetic standard. The amidated peptide was tested in a synthetic form to determine the antimicrobial activity towards the bacterial pathogens and insecticidal potential against pea aphids (). This peptide did not show antimicrobial activity but it significantly reduced the survival of aphids. It also increased the sensitivity of the aphids to two commonly used chemical insecticides (imidacloprid and methomyl). Since ant venom research is still in its infancy, the findings of this first study on venom peptides derived from highlight these insects as an important and rich source for discovery of novel lead structures with potential application in pest control.