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Molecular basis of the remarkable species selectivity of an insecticidal sodium channel toxin from the African spider Augacephalus ezendami

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Abstract
The inexorable decline in the armament of registered chemical insecticides has stimulated research into environmentally-friendly alternatives. Insecticidal spider-venom peptides are promising candidates for bioinsecticide development but it is challenging to find peptides that are specific for targeted pests. In the present study, we isolated an insecticidal peptide (Ae1a) from venom of the African spider Augacephalus ezendami (family Theraphosidae). Injection of Ae1a into sheep blowflies (Lucilia cuprina) induced rapid but reversible paralysis. In striking contrast, Ae1a was lethal to closely related fruit flies (Drosophila melanogaster) but induced no adverse effects in the recalcitrant lepidopteran pest Helicoverpa armigera. Electrophysiological experiments revealed that Ae1a potently inhibits the voltage-gated sodium channel BgNa(V)1 from the German cockroach Blattella germanica by shifting the threshold for channel activation to more depolarized potentials. In contrast, Ae1a failed to significantly affect sodium currents in dorsal unpaired median neurons from the American cockroach Periplaneta americana. We show that Ae1a interacts with the domain II voltage sensor and that sensitivity to the toxin is conferred by natural sequence variations in the S1-S2 loop of domain II. The phyletic specificity of Ae1a provides crucial information for development of sodium channel insecticides that target key insect pests without harming beneficial species.
Keywords
VENOM PEPTIDES, KNOCKDOWN-RESISTANCE, CRYSTAL-STRUCTURE, ARTHROPOD VENOMS, KNOTTIN PEPTIDE, VOLTAGE SENSORS, NEUROTOXIN, PHARMACOLOGY, REVEALS, PROTEIN

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Chicago
Herzig, Volker, Maria Ikonomopoulou, Jennifer J Smith, Slawomir Dziemborowicz, John Gilchrist, Lucia Kuhn-Nentwig, Fernanda Oliveira Rezende, et al. 2016. “Molecular Basis of the Remarkable Species Selectivity of an Insecticidal Sodium Channel Toxin from the African Spider Augacephalus Ezendami.” Scientific Reports 6.
APA
Herzig, Volker, Ikonomopoulou, M., Smith, J. J., Dziemborowicz, S., Gilchrist, J., Kuhn-Nentwig, L., Rezende, F. O., et al. (2016). Molecular basis of the remarkable species selectivity of an insecticidal sodium channel toxin from the African spider Augacephalus ezendami. SCIENTIFIC REPORTS, 6.
Vancouver
1.
Herzig V, Ikonomopoulou M, Smith JJ, Dziemborowicz S, Gilchrist J, Kuhn-Nentwig L, et al. Molecular basis of the remarkable species selectivity of an insecticidal sodium channel toxin from the African spider Augacephalus ezendami. SCIENTIFIC REPORTS. 2016;6.
MLA
Herzig, Volker, Maria Ikonomopoulou, Jennifer J Smith, et al. “Molecular Basis of the Remarkable Species Selectivity of an Insecticidal Sodium Channel Toxin from the African Spider Augacephalus Ezendami.” SCIENTIFIC REPORTS 6 (2016): n. pag. Print.
@article{8584509,
  abstract     = {The inexorable decline in the armament of registered chemical insecticides has stimulated research into environmentally-friendly alternatives. Insecticidal spider-venom peptides are promising candidates for bioinsecticide development but it is challenging to find peptides that are specific for targeted pests. In the present study, we isolated an insecticidal peptide (Ae1a) from venom of the African spider Augacephalus ezendami (family Theraphosidae). Injection of Ae1a into sheep blowflies (Lucilia cuprina) induced rapid but reversible paralysis. In striking contrast, Ae1a was lethal to closely related fruit flies (Drosophila melanogaster) but induced no adverse effects in the recalcitrant lepidopteran pest Helicoverpa armigera. Electrophysiological experiments revealed that Ae1a potently inhibits the voltage-gated sodium channel BgNa(V)1 from the German cockroach Blattella germanica by shifting the threshold for channel activation to more depolarized potentials. In contrast, Ae1a failed to significantly affect sodium currents in dorsal unpaired median neurons from the American cockroach Periplaneta americana. We show that Ae1a interacts with the domain II voltage sensor and that sensitivity to the toxin is conferred by natural sequence variations in the S1-S2 loop of domain II. The phyletic specificity of Ae1a provides crucial information for development of sodium channel insecticides that target key insect pests without harming beneficial species.},
  articleno    = {29538},
  author       = {Herzig, Volker and Ikonomopoulou, Maria and Smith, Jennifer J and Dziemborowicz, Slawomir and Gilchrist, John and Kuhn-Nentwig, Lucia and Rezende, Fernanda Oliveira and Moreira, Luciano Andrade and Nicholson, Graham M and Bosmans, Frank and King, Glenn F},
  issn         = {2045-2322},
  journal      = {SCIENTIFIC REPORTS},
  language     = {eng},
  pages        = {11},
  title        = {Molecular basis of the remarkable species selectivity of an insecticidal sodium channel toxin from the African spider Augacephalus ezendami},
  url          = {http://dx.doi.org/10.1038/srep29538},
  volume       = {6},
  year         = {2016},
}

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