Evidence map›Paper›PMID 35869123›Full record

ArticleScientific reports2022

Engineered chimeric insecticidal crystalline protein improves resistance to lepidopteran insects in rice (Oryza sativa L.) and maize (Zea mays L.).

Yang Liu, Siping Han, Shuo Yang, Ziqi Chen, Yuejia Yin, Jinghui Xi, Qing Liu, Weiyu Yan, Xinyuan Song, Fangfang Zhao and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
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

13 authors at 3 institutions in 1 country.

Yang Liu *Institute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Siping Han *Institute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Shuo YangCollege of Life Science, Jilin University, ChangChun, China.
Ziqi ChenInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Yuejia YinInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Jinghui XiCollege of Plant Science, Jilin University, ChangChun, China.
Qing LiuInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Weiyu YanInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Xinyuan SongInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Fangfang ZhaoCollege of Life Science and Technology, Harbin Normal University, Harbin, China.
Jia GuoInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China.
Xiangguo LiuInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China. lxgyyj@cjaas.com.
Dongyun HaoInstitute of Agricultural Biotechnology, Jilin Academy of Agricultural Sciences, Changchun, China. dyhao@cjaas.com.
Jilin Academy of Agricultural Sciences · CNJilin University · CNHarbin Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The insecticidal crystalline proteins (Crys) are a family of insect endotoxin functioning in crop protection. As insects keep evolving into tolerance to the existing Crys, it is necessary to discover new Cry proteins to overcome potential threatens. Crys possess three functional domains at their N-termini, and the most active region throughout evolution was found at the domain-III. We swapped domain-IIIs from various Cry proteins and generated seven chimeric proteins. All recombinants were expressed in Escherichia coli and their toxicity was assessed by dietary exposure assays. Three of the seven Crys exhibited a high toxicity to Asian corn borer over the controls. One of them, Cry1Ab-Gc, a chimeric Cry1Ab being replaced with the domain-III of Cry1Gc, showed the highest toxicity to rice stem borer when it was over-expressed in Oryza sativa. Furthermore, it was also transformed into maize, backcrossed into commercial maize inbred lines and then produced hybrid to evaluate their commercial value. Transgenic maize performed significant resistance to the Asian corn borer without affecting the yield. We further showed that this new protein did not have adverse effects on the environment. Our results indicated that domain III swapped of Crys could be used as an efficient method for developing new engineered insecticidal protein.

Indexed as

Bacillus thuringiensisInsecticidesOryzaAnimalsBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin ProteinsInsectaPlants, Genetically ModifiedRecombinant ProteinsZea maysBacillus thuringiensis ToxinsBacterial ProteinsEndotoxinsHemolysin ProteinsInsecticidesRecombinant Proteins

Identifiers

PMID35869123
PMCPMC9307649
OpenAlexW4286471240

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.