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ATP synthase subunit γ mediates Cry1Ac binding and toxicity in Grapholita molesta

Jiayang Feng1, Dandan Pan1, Yichen Wang1

  • 1Key Laboratory of Plant Protection Resources and Pest Management of Ministry of Education, Key Laboratory of Integrated Pest Management on Crops in Northwestern Loess Plateau of Ministry of Agriculture and Rural Affairs, College of Plant Protection, Northwest A&F University, Yangling, Shaanxi 712100, China.

Pesticide Biochemistry and Physiology
|September 7, 2025
PubMed

Insights

This study identifies GmolATPs-γ on the peritrophic membrane as a binding site for Bacillus thuringiensis (Bt) Cry1Ac toxin. Reducing GmolATPs-γ expression increases insect survival against Bt toxins, aiding pest control strategies.

Area of Science:

  • Entomology
  • Molecular Biology
  • Biochemistry

Background:

  • The insect peritrophic membrane (PM) is crucial for insect-microbe interactions.
  • Bacillus thuringiensis (Bt) Cry1Ac toxin is a key agent in insect pest control.
  • Understanding insect resistance mechanisms to Bt toxins is vital for effective pest management.

Purpose of the Study:

  • To investigate the role of the peritrophic membrane in Grapholita molesta (oriental fruit moth) resistance to Bacillus thuringiensis Cry1Ac toxin.
  • To identify specific proteins on the PM that interact with Cry1Ac.
  • To elucidate the functional significance of this interaction in larval susceptibility to Bt.

Main Methods:

  • Ligand blotting and mass spectrometry to identify Cry1Ac binding proteins on the PM.
  • RT-qPCR to analyze GmolATPs-γ gene expression in response to Cry1Ac exposure.
  • Homologous and heterologous competition assays to confirm binding specificity.
  • RNA interference (RNAi) to reduce GmolATPs-γ expression.
  • Heterologous expression in Sf9 cells to assess susceptibility.
  • In vivo experiments with larvae to evaluate mortality rates.

Main Results:

  • A protein, GmolATPs-γ, was identified as a specific binding partner for Cry1Ac on the PM of G. molesta.
  • GmolATPs-γ expression was downregulated upon Cry1Ac exposure.
  • Reduced GmolATPs-γ levels via RNAi significantly decreased larval mortality when treated with Cry1Ac.
  • Co-administration of Cry1Ac with GmolATPs-γ protein increased larval mortality.

Conclusions:

  • GmolATPs-γ physically binds to activated Cry1Ac toxin on the peritrophic membrane.
  • This interaction modulates Cry1Ac toxicity, influencing larval susceptibility.
  • Targeting GmolATPs-γ presents a potential strategy for enhancing Bt efficacy against G. molesta.
Keywords:
ATP synthase subunit γCry1AcGrapholita molestaPeritrophic membranes

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