CTLGA9 Interacts with ALP1 and APN Receptors To Modulate Cry11Aa Toxicity in Aedes aegypti

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.

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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