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Mutations of two acidic residues at the cytoplasmic end of segment IIIS6 of an insect sodium channel have distinct effects on pyrethroid resistance.

Publication ,  Journal Article
Chen, M; Du, Y; Nomura, Y; Zhu, G; Zhorov, BS; Dong, K
Published in: Insect biochemistry and molecular biology
March 2017

Mutations in sodium channels are known to confer knockdown resistance to pyrethroid insecticides, such as permethrin and cypermethrin, in various agricultural pests and disease vectors. Double mutations, D3i28V and E3i32G, were detected in cypermethrin-resistant Helicoverpa armigera and Heliothis virescens populations. However, the role of the two mutations in pyrethroid resistance remains unclear. In this study, we introduced the mutations into the cockroach sodium channel, BgNav1-1a, and examined their effects on channel gating and pyrethroid sensitivity in Xenopus oocytes. D3i28V alone and the double mutation, D3i28V/E3i32G, shifted the voltage dependence of activation in the depolarizing direction by 15 mV and 20 mV, respectively, whereas E3i32G had no significant effect. D3i28V reduced the amplitude of tail currents induced by permethrin and NRDC 157 (Type I pyrethroids) and deltamethrin and cypermethrin (Type II pyrethroids), whereas E3i32G alone had no effect. Intriguingly, the amplitude of Type II pyrethroid-induced tail current from D3i28V/E3i32G channels was similar to that of BgNav1-1a channels, but the decay of the tail currents was accelerated. Such effects were not observed for Type I pyrethroid-induced tail currents. Computational analysis based on the model of dual pyrethroid receptors on insect sodium channels predicted D3i28V and E3i32G exert their effects on channel gating and pyrethroid action via allosteric mechanisms. Our results not only illustrate the distinct effect of the D3i28V/E3i32G double mutations on Type I vs. Type II pyrethroids, but also reinforce the concept that accelerated decay of tail currents can be an effective mechanism of pyrethroid resistance to Type II pyrethroids.

Duke Scholars

Published In

Insect biochemistry and molecular biology

DOI

EISSN

1879-0240

ISSN

0965-1748

Publication Date

March 2017

Volume

82

Start / End Page

1 / 10

Related Subject Headings

  • Xenopus
  • Sodium Channels
  • Pyrethrins
  • Mutation
  • Insecticides
  • Insecticide Resistance
  • Insect Proteins
  • Entomology
  • Blattellidae
  • Animals
 

Citation

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Chen, M., Du, Y., Nomura, Y., Zhu, G., Zhorov, B. S., & Dong, K. (2017). Mutations of two acidic residues at the cytoplasmic end of segment IIIS6 of an insect sodium channel have distinct effects on pyrethroid resistance. Insect Biochemistry and Molecular Biology, 82, 1–10. https://doi.org/10.1016/j.ibmb.2017.01.007
Chen, Mengli, Yuzhe Du, Yoshiko Nomura, Guonian Zhu, Boris S. Zhorov, and Ke Dong. “Mutations of two acidic residues at the cytoplasmic end of segment IIIS6 of an insect sodium channel have distinct effects on pyrethroid resistance.Insect Biochemistry and Molecular Biology 82 (March 2017): 1–10. https://doi.org/10.1016/j.ibmb.2017.01.007.
Chen M, Du Y, Nomura Y, Zhu G, Zhorov BS, Dong K. Mutations of two acidic residues at the cytoplasmic end of segment IIIS6 of an insect sodium channel have distinct effects on pyrethroid resistance. Insect biochemistry and molecular biology. 2017 Mar;82:1–10.
Chen, Mengli, et al. “Mutations of two acidic residues at the cytoplasmic end of segment IIIS6 of an insect sodium channel have distinct effects on pyrethroid resistance.Insect Biochemistry and Molecular Biology, vol. 82, Mar. 2017, pp. 1–10. Epmc, doi:10.1016/j.ibmb.2017.01.007.
Chen M, Du Y, Nomura Y, Zhu G, Zhorov BS, Dong K. Mutations of two acidic residues at the cytoplasmic end of segment IIIS6 of an insect sodium channel have distinct effects on pyrethroid resistance. Insect biochemistry and molecular biology. 2017 Mar;82:1–10.
Journal cover image

Published In

Insect biochemistry and molecular biology

DOI

EISSN

1879-0240

ISSN

0965-1748

Publication Date

March 2017

Volume

82

Start / End Page

1 / 10

Related Subject Headings

  • Xenopus
  • Sodium Channels
  • Pyrethrins
  • Mutation
  • Insecticides
  • Insecticide Resistance
  • Insect Proteins
  • Entomology
  • Blattellidae
  • Animals