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Open AccessArticle

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

1
Bioresources Project Group, Fraunhofer Institute for Molecular Biology and Applied Ecology, Winchesterstrasse 2, 35394 Giessen, Germany
2
Institute for Insect Biotechnology, Justus Liebig University of Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany
*
Author to whom correspondence should be addressed.
Insects 2019, 10(2), 42; https://doi.org/10.3390/insects10020042
Received: 8 January 2019 / Revised: 21 January 2019 / Accepted: 24 January 2019 / Published: 1 February 2019
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 Myrmica rubra 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 (Acyrthosiphon pisum). 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 M. rubra highlight these insects as an important and rich source for discovery of novel lead structures with potential application in pest control. View Full-Text
Keywords: mass spectrometry; LC-MS; Formicidae; Myrmicinae; European fire ant; antimicrobial peptide; peptide toxin; bio-insecticide; aphids; Acyrthosiphon pisum mass spectrometry; LC-MS; Formicidae; Myrmicinae; European fire ant; antimicrobial peptide; peptide toxin; bio-insecticide; aphids; Acyrthosiphon pisum
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Heep, J.; Klaus, A.; Kessel, T.; Seip, M.; Vilcinskas, A.; Skaljac, M. Proteomic Analysis of the Venom from the Ruby Ant Myrmica rubra and the Isolation of a Novel Insecticidal Decapeptide. Insects 2019, 10, 42.

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