Cadherin AdCad1 in Alphitobius diaperinus larvae is a receptor of Cry3Bb toxin from Bacillus thuringiensis

Gang Hua1, Youngjin Park1, Michael J Adang2

  • 1Department of Entomology, University of Georgia, Athens, GA 30602-2603, USA.

Insights

Researchers identified a cadherin protein, AdCad1, as the first receptor for Bacillus thuringiensis (Bt) Cry3Bb toxin in lesser mealworm larvae. This discovery offers new strategies for pest control by targeting this specific toxin receptor.

Area of Science:

  • Insect toxicology
  • Molecular biology
  • Biochemistry

Background:

  • Bacillus thuringiensis (Bt) Cry proteins are crucial biopesticides targeting insect pests.
  • Cadherin proteins are known receptors for Cry toxins in various insect orders.
  • Understanding toxin-receptor interactions is key to developing effective pest management strategies.

Purpose of the Study:

  • To identify the specific receptor for Cry3Bb toxin in lesser mealworm (Alphitobius diaperinus) larvae.
  • To characterize the structure and function of the identified receptor.
  • To explore potential applications of this receptor in pest control.

Main Methods:

  • Identification and characterization of a 185 kDa cadherin (AdCad1) from A. diaperinus larvae.
  • Analysis of AdCad1 structural components (cadherin repeats - CR9, membrane-proximal extracellular domain - MPED).
  • Binding assays using Cry3Bb toxin and AdCad1 peptides.
  • RNA interference (RNAi) to silence AdCad1 expression.
  • Toxicity assays with Cry3Bb toxin and CR9 peptide.

Main Results:

  • AdCad1 was identified as the first receptor for Cry3Bb toxin in A. diaperinus.
  • AdCad1 possesses typical cadherin structural features, including CR9 and MPED regions.
  • CR9 and MPED peptides bound Cry3Bb toxin with high affinity and enhanced its toxicity.
  • Silencing AdCad1 significantly reduced larval susceptibility to Cry3Bb toxin.
  • Exogenous CR9 peptide restored Cry3Bb toxicity in RNAi-treated larvae.

Conclusions:

  • AdCad1 is a functional receptor for Cry3Bb toxin in lesser mealworm larvae.
  • The CR9 region of AdCad1 plays a critical role in Cry3Bb toxin binding.
  • Targeting AdCad1 or using CR9 peptides could be a novel strategy to overcome Cry3Bb resistance in insect pests.

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