Evidence map›Paper›PMID 24512949›Full record

ArticlePeptides2014

Membrane binding and oligomer membrane insertion are necessary but insufficient for Bacillus thuringiensis Cyt1Aa toxicity.

Pablo Emiliano Cantón, Jazmin A López-Díaz, Sarjeet S Gill, Alejandra Bravo, Mario Soberón

Abstract read
In one paragraph

Article in Peptides, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

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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

5 authors at 2 institutions in 2 countries.

Pablo Emiliano CantónInstituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca 62250, Morelos, Mexico. Electronic address: emiliano@ibt.unam.mx.
Jazmin A López-DíazInstituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca 62250, Morelos, Mexico. Electronic address: jazald@ibt.unam.mx.
Sarjeet S GillDepartment of Cell biology and Neuroscience, University of California, Riverside, CA 92521, United States. Electronic address: sarjeet.gill@ucr.edu.
Alejandra BravoInstituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca 62250, Morelos, Mexico. Electronic address: bravo@ibt.unam.mx.
Mario SoberónInstituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca 62250, Morelos, Mexico. Electronic address: mario@ibt.unam.mx.
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 2R01 AI066014-06NIAID NIH HHS R01 AI066014
6 · The paper itself

Abstract

Bacillus thuringiensis Cyt proteins are pore-forming toxins that have insecticidal activity mainly against dipteran insects. However, certain Cyt proteins have toxicity to some insect orders, but not toxicity of Cyt1Aa against lepidopteran larvae has been found. Insect specificity has been proposed to rely in specific binding to certain lipids on the brush border membrane of midgut cells since no protein receptors have been described so far. To determine the molecular basis of Cyt1Aa insect specificity we compared different steps of Cyt1Aa mode of action in a susceptible insect as the dipteran Aedes aegypti and also in the non-susceptible lepidopteran Manduca sexta. Our data shows that the lack toxicity of Cyt1Aa to M. sexta larvae does not rely on protoxin processing, membrane binding interaction, and oligomerization of Cyt1Aa since these steps were similar in the two insect species analyzed.

Indexed as

AedesAnimalsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin ProteinsHydrogen-Ion ConcentrationManducaMicrovilliPeptide HydrolasesProtein BindingProtein MultimerizationBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin Proteinsinsecticidal crystal protein, Bacillus ThuringiensisPeptide HydrolasesBacillus thuringiensisCyt toxinsMembrane bindingMode of actionOligomerization

Identifiers

PMID24512949
PMCPMC3927797
OpenAlexW2089677478

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.