ArticleInsect biochemistry and molecular biology2013
A 104 kDa Aedes aegypti aminopeptidase N is a putative receptor for the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis.
Article in Insect biochemistry and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Knockout of aminopeptidase N3 confers resistance to low concentrations of Bacillus thuringiensis Cry4Ba protoxin in Aedes aegypti.Parasites & vectors · 2026Article
- The Entomotoxic Fungal LectinJournal of agricultural and food chemistry · 2026Article
- Aedes aegypti strain selected with Bacillus thuringiensis svar. israelensis larvicide for 50 generations remains susceptible and exhibited increased fitness.Parasites & vectors · 2025Article
- Cry4Aa and Cry4Ba Mosquito-Active Toxins Utilize Different Domains in Binding to a ParticularToxins · 2022Article
- Function of CTLGA9 Amino Acid Residue Leucine-6 in Modulating Cry Toxicity.Frontiers in immunology · 2022Article
- Role of Lectin in the Response ofFrontiers in immunology · 2022Review
- Review
- Knockout of Two Cry-Binding Aminopeptidase N Isoforms Does Not Change Susceptibility ofInsects · 2021Article
- In vivo nanoscale analysis of the dynamic synergistic interaction of Bacillus thuringiensis Cry11Aa and Cyt1Aa toxins in Aedes aegypti.PLoS pathogens · 2021Article
- Cloning, expression and activity of ATP-binding protein in Bacillus thuringiensis toxicity modulation against Aedes aegypti.Parasites & vectors · 2019Article
- Article
- Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin.International journal of molecular sciences · 2017Article
- Aminopeptidase N1 is involved in Bacillus thuringiensis Cry1Ac toxicity in the beet armyworm, Spodoptera exigua.Scientific reports · 2017Article
- Proteomic analysis of Cry2Aa-binding proteins and their receptor function in Spodoptera exigua.Scientific reports · 2017Article
- Identification of protease m1 zinc metalloprotease conferring resistance to deltamethrin by characterization of an AFLP marker in Culex pipiens pallens.Parasites & vectors · 2016Article
- De Novo Assembly of the Transcriptome for Oriental Armyworm Mythimna separata (Lepidoptera: Noctuidae) and Analysis on Insecticide Resistance-Related Genes.Journal of insect science (Online) · 2016Article
- Article
- Alkaline phosphatases and aminopeptidases are altered in a Cry11Aa resistant strain of Aedes aegypti.Insect biochemistry and molecular biology · 2014Article
- Article
- Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Cry11Aa protein produced in Bacillus thuringiensis subsp. israelensis, a bacterial strain used worldwide for the control of Aedes aegypti larvae, binds midgut brush border membrane vesicles (BBMV) with an apparent K(d) of 29.8 nM. Previously an aminopeptidase N (APN), named AaeAPN2, was identified as a putative Cry11Aa toxin binding protein by pull-down assays using biotinylated Cry11Aa toxin (Chen et al., 2009. Insect Biochem. Mol. Biol. 39, 688-696). Here we show this protein localizes to the apical membrane of epithelial cells in proximal and distal regions of larval caeca. The AaeAPN2 protein binds Cry11Aa with high affinity, 8.6 nM. The full-length and fragments of AaeAPN2 were cloned and expressed in Escherichia coli. The toxin-binding region was identified and further competitive assays demonstrated that Cry11Aa binding to BBMV was efficiently competed by the full-length AaeAPN2 and the fragments of AaeAPN2b and AaeAPN2e. In bioassays against Ae. aegypti larvae, the presence of full-length and a partial fragment (AaeAPN2b) of AaeAPN2 enhanced Cry11Aa larval mortality. Taken together, we conclude that AaeAPN2 is a binding protein and plays a role in Cry11Aa toxicity.
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