Evidence map›Paper›PMID 20040372›Full record

ArticleInsect biochemistry and molecular biology2010

The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis.

Angeles Cancino-Rodezno, Cynthia Alexander, Roberto Villaseñor, Sabino Pacheco, Helena Porta, Yannick Pauchet, Mario Soberón, Sarjeet S Gill, Alejandra Bravo

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Insect biochemistry and molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

55 citing papers in PubMed, 106 citations in OpenAlex.

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  18. RNAi by SoakingInsects · 2021
    Article
  19. Response Mechanisms of Invertebrates toMicrobiology and molecular biology reviews : MMBR · 2021
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Angeles Cancino-RodeznoInstituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo Postal 510-3, Cuernavaca 62250, Morelos, Mexico.
Cynthia Alexander
Roberto Villaseñor
Sabino Pacheco
Helena Porta
Yannick Pauchet
Mario Soberón
Sarjeet S Gill
Alejandra Bravo
Universidad Nacional Autónoma de México · MXUniversity of California, Riverside · US

Funding

Mosquitocidal Action of Bacillus thuringiensis ToxinsR01AI066014 · NIAID · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI GILL, SARJEET S · 2005 to 2020
$6.4M
NIAID NIH HHS 1R01 AI066014NIAID NIH HHS R01 AI066014
6 · The paper itself

Abstract

The insecticidal Cry toxins are pore-forming toxins produced by the bacteria Bacillus thuringiensis that disrupt insect-midgut cells. In this work we analyzed the response of two different insect orders, the Lepidopteran Manduca sexta and Dipteran Aedes aegypti to highly specific Cry toxins, Cry1Ab and Cry11Aa, respectively. One pathway activated in different organisms in response to a variety of pore-forming toxins is the mitogen-activated protein kinase p38 pathway (MAPK p38) that activates a complex defense response. We analyzed the MAPK p38 activation by immunodetection of its phosphorylated isoform, and the induction of p38 by RT-PCR, real-time PCR quantitative assays and immunodetection. We show that MAPK p38 is activated at postraductional level after Cry toxin intoxication in both insect orders. We detected the p38 induction at the transcriptional and traductional level, and observed a different response. In these three levels, we found that both insects respond to Cry toxin action but M. sexta responses more strongly than A. aegypti. Gene silencing of MAPK p38 in vivo, resulted in both insect species becoming hypersensitive to Cry toxin action, suggesting that the MAPK p38 pathway is involved in insect defense against Bt Cry toxins. This finding may have biotechnological applications for enhancing the activity of some Bt Cry toxins against specific insect pests.

Indexed as

AedesAnimalsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin ProteinsInsect ProteinsMothsp38 Mitogen-Activated Protein KinasesSignal TransductionBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin Proteinsinsecticidal crystal protein, Bacillus ThuringiensisInsect Proteinsp38 Mitogen-Activated Protein Kinases

Identifiers

PMID20040372
PMCPMC2827608
OpenAlexW2000048938

What OpenQuestion holds

Textmetadata
LicenceTDM
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.