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Open AccessArticle

It Takes Two: Dimerization Is Essential for the Broad-Spectrum Predatory and Defensive Activities of the Venom Peptide Mp1a from the Jack Jumper Ant Myrmecia pilosula

1
Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia
2
CSIRO Agriculture and Food, St Lucia, QLD 4072, Australia
3
School of Pharmacy, The University of Queensland, Woolloongabba, QLD 4102, Australia
4
School of Science & Engineering, University of the Sunshine Coast, Sippy Downs, QLD 4556, Australia
*
Authors to whom correspondence should be addressed.
Biomedicines 2020, 8(7), 185; https://doi.org/10.3390/biomedicines8070185
Received: 11 June 2020 / Revised: 22 June 2020 / Accepted: 24 June 2020 / Published: 30 June 2020
(This article belongs to the Special Issue Animal Venoms–Curse or Cure?)
Ant venoms have recently attracted increased attention due to their chemical complexity, novel molecular frameworks, and diverse biological activities. The heterodimeric peptide ∆-myrtoxin-Mp1a (Mp1a) from the venom of the Australian jack jumper ant, Myrmecia pilosula, exhibits antimicrobial, membrane-disrupting, and pain-inducing activities. In the present study, we examined the activity of Mp1a and a panel of synthetic analogues against the gastrointestinal parasitic nematode Haemonchus contortus, the fruit fly Drosophila melanogaster, and for their ability to stimulate pain-sensing neurons. Mp1a was found to be both insecticidal and anthelmintic, and it robustly activated mammalian sensory neurons at concentrations similar to those reported to elicit antimicrobial and cytotoxic activity. The native antiparallel Mp1a heterodimer was more potent than heterodimers with alternative disulfide connectivity, as well as monomeric analogues. We conclude that the membrane-disrupting effects of Mp1a confer broad-spectrum biological activities that facilitate both predation and defense for the ant. Our structure–activity data also provide a foundation for the rational engineering of analogues with selectivity for particular cell types.
Keywords: ant; venom; venom peptide; pilosulin; heterodimer; antiparasitic; antimicrobial ant; venom; venom peptide; pilosulin; heterodimer; antiparasitic; antimicrobial
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MDPI and ACS Style

Nixon, S.A.; Dekan, Z.; Robinson, S.D.; Guo, S.; Vetter, I.; Kotze, A.C.; Alewood, P.F.; King, G.F.; Herzig, V. It Takes Two: Dimerization Is Essential for the Broad-Spectrum Predatory and Defensive Activities of the Venom Peptide Mp1a from the Jack Jumper Ant Myrmecia pilosula. Biomedicines 2020, 8, 185.

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