Evidence map›Paper›PMID 28539590›Full record

ArticleScientific reports2017

ABCC2 is associated with Bacillus thuringiensis Cry1Ac toxin oligomerization and membrane insertion in diamondback moth.

Josue Ocelotl, Jorge Sánchez, Isabel Gómez, Bruce E Tabashnik, Alejandra Bravo, Mario Soberón

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 60 citations in OpenAlex.

  1. Downregulation of APN1 andApplied and environmental microbiology · 2024
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  12. Review
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  15. Article
  16. Review
  17. Study of theToxins · 2020
    Article
  18. Article
  19. TheToxins · 2019
    Article
  20. Review
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

6 authors at 2 institutions in 2 countries.

Josue OcelotlInstituto de Biotecnología, Universidad Nacional Autónoma de México. Apdo. Postal 510-3, Cuernavaca, Mor. 62210, Mexico.
Jorge SánchezInstituto de Biotecnología, Universidad Nacional Autónoma de México. Apdo. Postal 510-3, Cuernavaca, Mor. 62210, Mexico.
Isabel GómezInstituto de Biotecnología, Universidad Nacional Autónoma de México. Apdo. Postal 510-3, Cuernavaca, Mor. 62210, Mexico.
Bruce E TabashnikDepartment of Entomology, University of Arizona, Tucson, Arizona, USA.ORCID 0000-0002-2430-2367
Alejandra BravoInstituto de Biotecnología, Universidad Nacional Autónoma de México. Apdo. Postal 510-3, Cuernavaca, Mor. 62210, Mexico.
Mario SoberónInstituto de Biotecnología, Universidad Nacional Autónoma de México. Apdo. Postal 510-3, Cuernavaca, Mor. 62210, Mexico. mario@ibt.unam.mx.
Universidad Nacional Autónoma de México · MXUniversity of Arizona · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cry1A insecticidal toxins bind sequentially to different larval gut proteins facilitating oligomerization, membrane insertion and pore formation. Cry1Ac interaction with cadherin triggers oligomerization. However, a mutation in an ABC transporter gene (ABCC2) is linked to Cry1Ac resistance in Plutella xylostella. Cry1AcMod, engineered to lack helix α-1, was able to form oligomers without cadherinbinding and effectively countered Cry1Ac resistance linked to ABCC2. Here we analyzed Cry1Ac and Cry1AcMod binding and oligomerization by western blots using brush border membrane vesicles (BBMV) from a strain of P. xylostella susceptible to Cry1Ac (Geneva 88) and a strain with resistance to Cry1Ac (NO-QAGE) linked to an ABCC2 mutation. Resistance correlated with lack of specific binding and reduced oligomerization of Cry1Ac in BBMV from NO-QAGE. In contrast, Cry1AcMod bound specifically and still formed oligomers in BBMV from both strains. We compared association of pre-formed Cry1Ac oligomer, obtained by incubating Cry1Ac toxin with a Manduca sexta cadherin fragment, with BBMV from both strains. Our results show that pre-formed oligomers associate more efficiently with BBMV from Geneva 88 than with BBMV from NO-QAGE, indicating that the ABCC2 mutation also affects the association of Cry1Ac oligomer with the membrane. These data indicate, for the first time, that ABCC2 facilitates Cry1Ac oligomerization and oligomer membrane insertion in P. xylostella.

Indexed as

AnimalsATP-Binding Cassette, Sub-Family C ProteinsBacillus thuringiensis ToxinsBacterial ProteinsBiological Control AgentsCell-Derived MicroparticlesCell MembraneEndotoxinsHemolysin ProteinsInsecticide ResistanceInsecticidesInsect ProteinsLarvaManducaMicrovilliMothsATP-Binding Cassette, Sub-Family C ProteinsBacillus thuringiensis ToxinsBacterial ProteinsBiological Control AgentsEndotoxinsHemolysin Proteinsinsecticidal crystal protein, Bacillus ThuringiensisInsecticidesInsect ProteinsMultidrug Resistance-Associated Protein 2Protein Isoforms

Identifiers

PMID28539590
PMCPMC5443830
OpenAlexW2615772358

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.