CTLGA9 Interacts with ALP1 and APN Receptors To Modulate Cry11Aa Toxicity in Aedes aegypti
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Updated: Jan 21, 2026

Maintaining Aedes aegypti Mosquitoes Infected with Wolbachia
Published on: August 14, 2017
Khadija Batool1, Intikhab Alam2, Liang Jin1
1State Key Laboratory of Ecological Pest Control for Fujian and Taiwan Crops, College of Life Sciences, Key Lab of Biopesticides and Chemical Biology, MOE , Fujian Agriculture and Forestry University , 350002 Fuzhou , Fujian , PR China.
Abstract:
The mosquito Aedes aegypti is associated with the spread of many viral diseases in humans, including Dengue virus (DENVs), Yellow fever virus (YFV), Zika virus (ZIKV), and Chikungunya virus (CHIKV). Bacillus thuringiensis (Bt) is widely used as a biopesticide, which produces Cry toxins for mosquito control. The Cry toxins bind mainly to important receptors, including alkaline phosphatase (ALP) and aminopeptidase-N (APN). This work investigated the function of a C-type lectin, CTLGA9, in A. aegypti in response to Cry toxins. Our results showed by far-western blot and ELISA methods that the CTLTGA9 protein interacted with brush border membrane vesicles (BBMVs) of A. aegypti larvae and with ALP1, APN, and Cry11Aa proteins. Furthermore, molecular docking showed overlapping binding sites in ALP1 and APN for binding to Cry11Aa and CTLGA9. The toxicity assays further demonstrated that CTLGA9 inhibited the larvicidal activity of Cry toxins. According to the results of molecular docking, CTLGA9 may compete with Cry11Aa for binding to ALP1 and APN receptors and thus decreases the mosquitocidal toxicity of Cry11Aa. Our results provide further insights into better understanding the mechanism of Cry toxins and help improve the Cry toxicity for mosquito control.
Insights
A newly identified C-type lectin, CTLGA9, in Aedes aegypti mosquitoes interferes with Bacillus thuringiensis Cry toxins. This interaction reduces mosquito larvicidal activity, offering new strategies for disease vector control.
Area of Science:
- Entomology
- Molecular Biology
- Biochemistry
Background:
- Aedes aegypti mosquitoes transmit numerous human viral diseases like Dengue, Zika, and Chikungunya.
- Bacillus thuringiensis (Bt) produces Cry toxins, a biopesticide targeting mosquito larvae by binding to receptors like alkaline phosphatase (ALP) and aminopeptidase-N (APN).
Purpose of the Study:
- To investigate the role of the C-type lectin CTLGA9 in Aedes aegypti in response to Bacillus thuringiensis Cry toxins.
- To elucidate the molecular mechanisms underlying the interaction between CTLGA9 and Cry toxins.
Main Methods:
- Far-western blot and ELISA were used to determine protein interactions.
- Brush border membrane vesicles (BBMVs) from A. aegypti larvae were utilized.
- Molecular docking simulations were performed to analyze binding site interactions.
- Larvicidal toxicity assays were conducted to assess the impact on Cry toxin efficacy.
Main Results:
- The CTLGA9 protein was found to interact with A. aegypti larval BBMVs, specifically with ALP1, APN, and Cry11Aa proteins.
- Molecular docking revealed overlapping binding sites for CTLGA9 and Cry11Aa on ALP1 and APN.
- CTLGA9 significantly inhibited the larvicidal activity of Cry toxins.
Conclusions:
- CTLGA9 acts as an antagonist to Cry toxins by competing for binding to ALP1 and APN receptors in A. aegypti.
- This competitive inhibition reduces the mosquitocidal efficacy of Cry toxins.
- Understanding CTLGA9's function provides insights into Cry toxin mechanisms and potential improvements for mosquito control strategies.
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