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Related Experiment Video

Updated: May 12, 2026

Analysis of Gene Expression in Emerald Ash Borer (Agrilus planipennis) Using Quantitative Real Time-PCR
11:22

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Published on: May 5, 2010

New Insight into FKBP12's Involvement in Cry1Ac-Induced Toxicity to Helicoverpa armigera.

Pin Li1, Shuo Yang1, Guoping Li2

  • 1State Key Laboratory of High-Efficiency Production of Wheat-Maize Double Cropping/College of Plant Protection, Henan Agricultural University, Zhengzhou 450046, China.

Journal of Agricultural and Food Chemistry
|February 10, 2026
PubMed
Summary

FKBP12 (FK506-binding protein) regulates ABCC2 transporter activity, influencing the toxicity of Cry1Ac in insects. This discovery offers new strategies for managing pesticide resistance in agricultural pests.

Keywords:
ABCC2Bacillus thuringiensisFKBP12Helicoverpa armigeratoxicity

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Last Updated: May 12, 2026

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04:51

Developing a Feeding Assay System for Evaluating the Insecticidal Effect of Phytochemicals on Helicoverpa armigera

Published on: May 26, 2023

Area of Science:

  • Molecular Biology
  • Insect Toxicology
  • Biochemistry

Background:

  • FKBP12 (FK506-binding protein) is crucial for insect development and ABC transporter regulation.
  • Previous studies indicated FK506 enhances Cry1Ac toxicity in *Helicoverpa armigera*.
  • A hypothesis proposed FKBP12-FK506 interaction disrupts ABCC2 function, affecting Cry1Ac toxicity.

Purpose of the Study:

  • To investigate the role of FKBP12 in Cry1Ac toxicity.
  • To examine the interaction between FKBP12 and ABCC2.
  • To understand the mechanism of FKBP12 in modulating insect susceptibility to Bt toxins.

Main Methods:

  • Gene expression analysis of FKBP12 and ABCC2 in *H. armigera*.
  • RNA interference (RNAi) to silence *HaFKBP12* in *H. zea* midgut cells.
  • Heterologous expression of FKBP12 and ABCC2 in Sf9 cells to assess functional interactions.

Main Results:

  • Both FKBP12 and ABCC2 were downregulated in Cry1Ac-exposed and resistant *H. armigera*.
  • Silencing *HaFKBP12* reduced *H. zea* midgut cell susceptibility to Cry1Ac.
  • Overexpression of FKBP12 increased insect cell susceptibility to Cry1Ac and directly modulated ABCC2 transport activity.

Conclusions:

  • FKBP12 directly binds and regulates ABCC2 activity, influencing Cry1Ac toxicity.
  • This interaction provides a mechanism for FKBP12 in modulating insect response to Bt toxins.
  • Findings suggest FKBP12-ABCC2 interaction as a target for novel insecticide development and resistance management strategies.