Evidence map›Paper›PMID 24454741›Full record

ArticlePloS one2014

Bioaccumulation of Cry1Ab protein from an herbivore reduces anti-oxidant enzyme activities in two spider species.

Ji Zhou, Kaifu Xiao, Baoyang Wei, Zhi Wang, Yun Tian, Yixing Tian, Qisheng Song

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 25 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

7 authors at 1 institution in 2 countries.

Ji ZhouCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Kaifu XiaoCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Baoyang WeiCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Zhi WangCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Yun TianCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Yixing TianCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Qisheng SongCollege of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China ; Division of Plant Sciences, University of Missouri, Columbia, Missouri, United States of America.
Hunan Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cry proteins are expressed in rice lines for lepidopteran pest control. These proteins can be transferred from transgenic rice plants to non-target arthropods, including planthoppers and then to a predatory spider. Movement of Cry proteins through food webs may reduce fitness of non-target arthropods, although recent publications indicated no serious changes in non-target populations. Nonetheless, Cry protein intoxication influences gene expression in Cry-sensitive insects. We posed the hypothesis that Cry protein intoxication influences enzyme activities in spiders acting in tri-trophic food webs. Here we report on the outcomes of experiments designed to test our hypothesis with two spider species. We demonstrated that the movement of CryAb protein from Drosophila culture medium into fruit flies maintained on the CryAb containing medium and from the flies to the spiders Ummeliata insecticeps and Pardosa pseudoannulata. We also show that the activities of three key metabolic enzymes, acetylcholine esterase (AchE), glutathione peroxidase (GSH-Px), and superoxide dismutase (SOD) were significantly influenced in the spiders after feeding on Cry1Ab-containing fruit flies. We infer from these data that Cry proteins originating in transgenic crops impacts non-target arthropods at the physiological and biochemical levels, which may be one mechanism of Cry protein-related reductions in fitness of non-target beneficial predators.

Indexed as

AcetylcholinesteraseAnimalsAntioxidantsBacillus thuringiensis ToxinsBacterial ProteinsCulture MediaDrosophila melanogasterEndotoxinsGlutathione PeroxidaseHemolysin ProteinsHerbivorySpidersSuperoxide DismutaseAcetylcholinesteraseAntioxidantsBacillus thuringiensis ToxinsBacterial ProteinsCulture MediaEndotoxinsGlutathione PeroxidaseHemolysin Proteinsinsecticidal crystal protein, Bacillus ThuringiensisSuperoxide Dismutase

Identifiers

PMID24454741
PMCPMC3890278
OpenAlexW1963846127

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.