Evidence map›Paper›PMID 21844358›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Differential alteration of two aminopeptidases N associated with resistance to Bacillus thuringiensis toxin Cry1Ac in cabbage looper.

Kasorn Tiewsiri, Ping Wang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
7.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

82 citing papers in PubMed, 203 citations in OpenAlex.

  1. A second locus associated with high-level resistance to Bt Cry1Ac inApplied and environmental microbiology · 2026
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  2. Review
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  4. Downregulation of APN1 andApplied and environmental microbiology · 2024
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  9. Downregulation of a transcription factor associated with resistance to Bt toxin Vip3Aa in the invasive fall armyworm.Proceedings of the National Academy of Sciences of the United States of America · 2023
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22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Kasorn TiewsiriDepartment of Entomology, Cornell University, New York State Agricultural Experiment Station, Geneva, NY 14456, USA.
Ping Wang
New York State Department of Agriculture and Markets · USUniversity of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The soil bacterium Bacillus thuringiensis (Bt) is the most successfully used biopesticide in agriculture, and its insecticidal protein genes are the primary transgenes used for insect control in transgenic crops. However, evolution of insect resistance to Bt toxins threatens the long-term future of Bt applications. To date, cases of resistance to Bt toxins have been reported in agricultural situations in six insect species, but the molecular basis for these cases of resistance remains unclear. Here we report that the resistance to the Bt toxin Cry1Ac in the cabbage looper, Trichoplusia ni, evolved in greenhouses, is associated with differential alteration of two midgut aminopeptidases N, APN1 and APN6, conferred by a trans-regulatory mechanism. Biochemical, proteomic, and molecular analyses showed that in the Cry1Ac-resistant T. ni, APN1 was significantly down-regulated, whereas APN6 was significantly up-regulated. The Cry1Ac resistance was correlated with down-regulation of APN1 but not with the up-regulation of APN6. The concurrent up-regulation of APN6 and down-regulation of APN1 might play a role in compensating for the loss of APN1 to minimize the fitness costs of the resistance. Along with identifying reduced expression of APN1 as the molecular basis of Bt resistance selected in an agricultural setting, our findings demonstrate the importance of APN1 to the mode of action of Bt toxin Cry1Ac.

Indexed as

AnimalsBacillus thuringiensisBacillus thuringiensis ToxinsBacterial ProteinsBrassicaCD13 AntigensDigestive SystemElectrophoresis, Polyacrylamide GelEndotoxinsGene Expression ProfilingGene Expression Regulation, EnzymologicGenes, InsectGenetic LinkageHemolysin ProteinsInsecticide ResistanceInsect ProteinsBacillus thuringiensis ToxinsBacterial ProteinsCD13 AntigensEndotoxinsHemolysin Proteinsinsecticidal crystal protein, Bacillus ThuringiensisInsect ProteinsRNA, Messenger

Identifiers

PMID21844358
PMCPMC3161562
OpenAlexW2064458603

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.