Evidence map›Paper›PMID 26760761›Full record

ArticlePloS one2016

Production of Biologically Active Cecropin A Peptide in Rice Seed Oil Bodies.

Laura Montesinos, Mireia Bundó, Esther Izquierdo, Sonia Campo, Esther Badosa, Michel Rossignol, Emilio Montesinos, Blanca San Segundo, María Coca

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.8field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 34 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

9 authors at 3 institutions in 2 countries.

Laura MontesinosInstitute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, Girona, Spain.
Mireia BundóCentre for Research in Agricultural Genomics (CRAG), CSIC-IRTA-UAB-UB, Edifici CRAG, Campus de la UAB, Bellaterra, Barcelona, Spain.
Esther IzquierdoMass Spectrometry Proteomics Platform, Biochimie et Physiologie Moléculaire des Plantes, SupAgro/INRA/CNRS/UMII/UMR 5004, Montpellier, France.
Sonia CampoCentre for Research in Agricultural Genomics (CRAG), CSIC-IRTA-UAB-UB, Edifici CRAG, Campus de la UAB, Bellaterra, Barcelona, Spain.
Esther BadosaInstitute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, Girona, Spain.
Michel RossignolMass Spectrometry Proteomics Platform, Biochimie et Physiologie Moléculaire des Plantes, SupAgro/INRA/CNRS/UMII/UMR 5004, Montpellier, France.
Emilio MontesinosInstitute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, Girona, Spain.
Blanca San SegundoCentre for Research in Agricultural Genomics (CRAG), CSIC-IRTA-UAB-UB, Edifici CRAG, Campus de la UAB, Bellaterra, Barcelona, Spain.
María CocaCentre for Research in Agricultural Genomics (CRAG), CSIC-IRTA-UAB-UB, Edifici CRAG, Campus de la UAB, Bellaterra, Barcelona, Spain.
Center for Research in Agricultural Genomics · ESUniversity of Girona · ESInstitut des Sciences des Plantes de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cecropin A is a natural antimicrobial peptide that exhibits fast and potent activity against a broad spectrum of pathogens and neoplastic cells, and that has important biotechnological applications. However, cecropin A exploitation, as for other antimicrobial peptides, is limited by their production and purification costs. Here, we report the efficient production of this bioactive peptide in rice bran using the rice oleosin 18 as a carrier protein. High cecropin A levels were reached in rice seeds driving the expression of the chimeric gene by the strong embryo-specific oleosin 18 own promoter, and targeting the peptide to the oil body organelle as an oleosin 18-cecropin A fusion protein. The accumulation of cecropin A in oil bodies had no deleterious effects on seed viability and seedling growth, as well as on seed yield. We also show that biologically active cecropin A can be easily purified from the transgenic rice seeds by homogenization and simple flotation centrifugation methods. Our results demonstrate that the oleosin fusion technology is suitable for the production of cecropin A in rice seeds, which can potentially be extended to other antimicrobial peptides to assist their exploitation.

Indexed as

Amino Acid SequenceAntimicrobial Cationic PeptidesGenome, PlantLipid DropletsMass SpectrometryMolecular Sequence DataOryzaPhenotypePlant OilsPlant ProteinsPlants, Genetically ModifiedPromoter Regions, GeneticRecombinant Fusion ProteinsSeedsTransgenesAntimicrobial Cationic Peptidescecropin Aoleosin protein, Oryza sativaPlant OilsPlant ProteinsRecombinant Fusion Proteins

Identifiers

PMID26760761
PMCPMC4711921
OpenAlexW2238563159

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.