Identification and functional characterization of a novel insecticidal decapeptide from the myrmicine ant manica rubida
Autor: | Tobias Kessel, Maximilian Seip, Jens Grotmann, Andreas Vilcinskas, Marisa Skaljac, Henrike Schmidtberg, John Heep |
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Přispěvatelé: | Publica |
Jazyk: | angličtina |
Rok vydání: | 2019 |
Předmět: |
0106 biological sciences
Insecticides antimicrobial peptide Health Toxicology and Mutagenesis media_common.quotation_subject lcsh:Medicine Venom Insect Manica rubida Toxicology 01 natural sciences Ant venom complex mixtures Article 03 medical and health sciences medicine Animals Amino Acid Sequence myrmica rubra Formicidae 030304 developmental biology media_common mass spectrometry acyrthosiphon pisum 0303 health sciences Hemolymph coagulation Aphid Wound Healing venom gland biology Ant Venoms lcsh:R fungi Acyrthosiphon pisum food and beverages biology.organism_classification medicine.disease ANT LC-MS Myrmicinae Myrmica rubra bioinsecticide aphids 010602 entomology Biochemistry Oligopeptides |
Zdroj: | Toxins Toxins, Vol 11, Iss 10, p 562 (2019) Volume 11 Issue 10 |
Popis: | Ant venoms contain many small, linear peptides, an untapped source of bioactive peptide toxins. The control of agricultural insect pests currently depends primarily on chemical insecticides, but their intensive use damages the environment and human health, and encourages the emergence of resistant pest populations. This has promoted interest in animal venoms as a source of alternative, environmentally-friendly bio-insecticides. We tested the crude venom of the predatory ant, Manica rubida, and observed severe fitness costs in the parthenogenetic pea aphid (Acyrthosiphon pisum), a common agricultural pest. Therefore, we explored the M. rubida venom peptidome and identified a novel decapeptide U-MYRTX-MANr1 (NH2-IDPKVLESLV-CONH2) using a combination of Edman degradation and de novo peptide sequencing. Although this myrmicitoxin was inactive against bacteria and fungi, it reduced aphid survival and reproduction. Furthermore, both crude venom and U-MYRTX-MANr1 reversibly paralyzed injected aphids and induced a loss of body fluids. Components of M. rubida venom may act on various biological targets including ion channels and hemolymph coagulation proteins, as previously shown for other ant venom toxins. The remarkable insecticidal activity of M. rubida venom suggests it may be a promising source of additional bio-insecticide leads. |
Databáze: | OpenAIRE |
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