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.
Abstract:
Bacillus thuringiensis (Bt) Cry proteins are used as components of biopesticides or expressed in transgenic crops to control diverse insect pests worldwide. These Cry toxins bind to receptors on the midgut brush border membrane and kill enterocytes culminating in larval mortality. Cadherin proteins have been identified as Cry toxin receptors in diverse lepidopteran, coleopteran, and dipteran species. In the present work we report a 185 kDa cadherin (AdCad1) from larvae of the lesser mealworm (Alphitobius diaperinus) larvae as the first identified receptor for Cry3Bb toxin. The AdCad1 protein contains typical structural components for Cry toxin receptor cadherins, including nine cadherin repeats (CR9), a membrane-proximal extracellular domain (MPED) and a cytosolic region. Peptides corresponding to the CR9 and MPED regions bound Cry3Bb toxin with high affinities (23 nM and 40 nM) and significantly synergized Cry3Bb toxicity against A. diperinus larvae. Silencing of AdCad1 expression through RNA interference resulted in highly reduced susceptibility to Cry3Bb in A. diperinus larvae. The CR9 peptide fed with toxin to RNAi-treated larvae restored Cry3Bb toxicity. These results are evidences that AdCad1 is a functional receptor of Cry3Bb toxin and that exogenously fed CR9 peptide can overcome the effect of reduced AdCad1expression on Cry3Bb toxicity to larvae.
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.
Related Concept Videos
Cadherins in Tissue Organization
Cell Sorting During Development
Cell sorting plays an...
Structure of Cadherins
Adherens Junctions
Adherens Junctions are Dynamic
Role Of Notch Signalling In Intestinal Stem Cell Renewal
Direct cell-to-cell contact is needed for the activation of Notch signaling. The signal is initiated when a notch ligand binds to a receptor on an adjacent cell, also...
Hedgehog Signaling Pathway
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal


