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Area of Science:

  • Insect molecular biology
  • Neuroscience
  • Structural biology

Background:

  • Insect transient receptor potential vanilloid-type (TRPV) channels, Nanchung (Nan) and Inactive (Iav), are crucial for mechanosensation and are insecticide targets.
  • Afidopyropen (AP) is an insecticide effective against hemipteran insects that disrupts chordotonal organ function, but its precise mechanism of action on Nan-Iav channels is unknown.
  • Understanding Nan-Iav channel assembly, modulator binding, and calcium-dependent regulation is essential for developing new insecticides.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying insecticide and agonist interactions with insect Nan-Iav TRPV channels.
  • To determine the structural basis for Nan-Iav channel assembly and regulation by calcium and calmodulin.
  • To provide insights for the rational design of novel insecticides targeting insect TRPV channels.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structures of hemipteran Nan-Iav channels.
  • Structures were solved in the apo state with bound calmodulin, and in complex with the insecticide afidopyropen (AP) and the agonist nicotinamide (NAM).
  • Analysis focused on interactions within the cytosolic ankyrin repeat domain (ARD) interfaces.

Main Results:

  • The cryo-EM structures reveal the binding sites of AP and NAM within the cytosolic ARD interfaces of Nan-Iav channels.
  • Unexpectedly, Nanchung (Nan) channels alone were observed to form a pentamer, stabilized by AP-mediated ARD interactions.
  • Calmodulin was observed bound in the apo state, suggesting a role in channel regulation.

Conclusions:

  • The ankyrin repeat domain (ARD) plays a critical role in Nan-Iav channel assembly and function, as well as in mediating interactions with insecticides and agonists.
  • The findings provide a molecular understanding of how afidopyropen (AP) and nicotinamide (NAM) interact with Nan-Iav channels, paving the way for new insecticide development.
  • Further investigation into calcium-dependent regulation and the role of calmodulin is warranted.