ArticleScientific reports2016
APN1 is a functional receptor of Cry1Ac but not Cry2Ab in Helicoverpa zea.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Knockout of aminopeptidase N3 confers resistance to low concentrations of Bacillus thuringiensis Cry4Ba protoxin in Aedes aegypti.Parasites & vectors · 2026Article
- Novel codon-optimized cry1Ac34 gene from Indian Bt isolate confers resistance against Helicoverpa armigera in Transgenic tobacco.Archives of microbiology · 2026Article
- Mismatch between lab-generated and field-evolved resistance to transgenic Bt crops inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Performance insights into spray-dryer microencapsulated Bacillus thuringiensis cry pesticidal proteins with gum arabic and maltodextrin for effective pest control.Applied microbiology and biotechnology · 2024Article
- Analysis of the Effect ofToxins · 2023Article
- Genome evolution in an agricultural pest following adoption of transgenic crops.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Novel Reference for Bt-Resistance Mechanism inInsects · 2021Article
- Knockout of Two Cry-Binding Aminopeptidase N Isoforms Does Not Change Susceptibility ofInsects · 2021Article
- Suppression of Calcineurin Enhances the Toxicity of Cry1Ac toFrontiers in microbiology · 2021Article
- Differences in midgut transcriptomes between resistant and susceptible strains of Chilo suppressalis to Cry1C toxin.BMC genomics · 2020Article
- Transcriptomic Responses to Different Cry1Ac Selection Stresses inFrontiers in physiology · 2018Article
- Specific Binding Protein ABCC1 Is Associated With Cry2Ab Toxicity inFrontiers in physiology · 2018Article
- Functional roles of cadherin, aminopeptidase-N and alkaline phosphatase from Helicoverpa armigera (Hübner) in the action mechanism of Bacillus thuringiensis Cry2Aa.Scientific reports · 2017Article
- Aminopeptidase N1 is involved in Bacillus thuringiensis Cry1Ac toxicity in the beet armyworm, Spodoptera exigua.Scientific reports · 2017Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lepidopteran midgut aminopeptidases N (APNs) are phylogenetically divided into eight clusters, designated as APN1-8. Although APN1 has been implicated as one of the receptors for Cry1Ac in several species, its potential role in the mode of action of Cry2Ab has not been functionally determined so far. To test whether APN1 also acts as one of the receptors for Cry1Ac in Helicoverpa zea and even for Cry2Ab in this species, we conducted a gain of function analysis by heterologously expressing H. zea APN1 (HzAPN1) in the midgut and fat body cell lines of H. zea and the ovarian cell line of Spodoptera frugiperda (Sf9) and a loss of function analysis by RNAi (RNA interference) silencing of the endogenous APN1 in the three cell lines using the HzAPN1 double strand RNA (dsRNA). Heterologous expression of HzAPN1 significantly increased the susceptibility of the three cell lines to Cry1Ac, but had no effects on their susceptibility to Cry2Ab. Knocking down of the endogenous APN1 made the three cell lines resistant to Cry1Ac, but didn't change cell lines susceptibility to Cry2Ab. The findings from this study demonstrate that HzAPN1 is a functional receptor of Cry1Ac, but not Cry2Ab.
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