ArticleParasites & vectors2026
Knockout of aminopeptidase N3 confers resistance to low concentrations of Bacillus thuringiensis Cry4Ba protoxin in Aedes aegypti.
Article in Parasites & vectors, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundBacillus thuringiensis is widely employed for biological control. It can effectively suppress populations of various mosquito species, including Aedes aegypti. However, the precise mechanism underlying the action of Cry protein produced by Bacillus thuringiensis on Ae. aegypti remains elusive. On the basis of our previous research findings, five Aedes aminopeptidase N proteins (AeAPNs) were identified from the brush border membrane vesicles (BBMV) of Ae. aegypti that could bind to Cry4Ba or Cry11Aa. Further analysis confirmed that AeAPN1 and AeAPN2 are not functional receptors for these proteins. In this study, we investigated an additional aminopeptidase N (AeAPN3, AAEL012774) as a potential binding receptor for Cry proteins.
methodsComprehensive bioinformatics analysis involving whole-genome screening, genetic mapping, structural characterization, phylogenetic analysis, and spatiotemporal expression profiling were used to identify Ae. aegypti aminopeptidase N homologs. Ligand blotting and enzyme-linked immunosorbent assay (ELISA) were used to measure binding affinity to Cry4Ba. To elucidate its functional role as a potential receptor mediating Cry4Ba activity in Ae. aegypti midgut cells, AeAPN3 was knocked out with CRISPR/Cas9 technology.
resultsA total of 29 homologs of Ae. aegypti aminopeptidase N were identified in this study. Then, we expressed GST-APN3 fusion protein in E. coli and found that it had high-affinity binding to Cry4Ba protein (K
conclusionsOverall, this study provides a foundation for elucidating the specific larvicidal mechanisms of Bacillus thuringiensis (Bt) against mosquito populations.
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