Evidence map›Paper›PMID 24376887›Full record

ArticlePloS one2013

Derivatives of the antimicrobial peptide BP100 for expression in plant systems.

Esther Badosa, Gemma Moiset, Laura Montesinos, Montserrat Talleda, Eduard Bardají, Lidia Feliu, Marta Planas, Emilio Montesinos

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Deciphering the Mechanism of Action of the Antimicrobial Peptide BP100.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Frontiers in plant science · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. A Synergic Potential of Antimicrobial Peptides againstMolecules (Basel, Switzerland) · 2021
    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

8 authors at 1 institution in 1 country.

Esther BadosaLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, Campus Montilivi, Girona, Spain.
Gemma MoisetLIPPSO, Department of Chemistry, University of Girona, Campus Montilivi, Girona, Spain.
Laura MontesinosLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, Campus Montilivi, Girona, Spain.
Montserrat TalledaLIPPSO, Department of Chemistry, University of Girona, Campus Montilivi, Girona, Spain.
Eduard BardajíLIPPSO, Department of Chemistry, University of Girona, Campus Montilivi, Girona, Spain.
Lidia FeliuLIPPSO, Department of Chemistry, University of Girona, Campus Montilivi, Girona, Spain.
Marta PlanasLIPPSO, Department of Chemistry, University of Girona, Campus Montilivi, Girona, Spain.
Emilio MontesinosLaboratory of Plant Pathology, Institute of Food and Agricultural Technology-CIDSAV-XaRTA, University of Girona, Campus Montilivi, Girona, Spain.
University of Girona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Production of antimicrobial peptides in plants constitutes an approach for obtaining them in high amounts. However, their heterologous expression in a practical and efficient manner demands some structural requirements such as a minimum size, the incorporation of retention signals to assure their accumulation in specific tissues, and the presence of protease cleavage amino acids and of target sequences to facilitate peptide detection. Since any sequence modification may influence the biological activity, peptides that will be obtained from the expression must be screened prior to the synthesis of the genes for plant transformation. We report herein a strategy for the modification of the antimicrobial undecapeptide BP100 that allowed the identification of analogues that can be expressed in plants and exhibit optimum biological properties. We prepared 40 analogues obtained by incorporating repeated units of the antimicrobial undecapeptide, fragments of natural peptides, one or two AGPA hinges, a Gly or Ser residue at the N-terminus, and a KDEL fragment and/or the epitope tag54 at the C-terminus. Their antimicrobial, hemolytic and phytotoxic activities, and protease susceptibility were evaluated. Best sequences contained a magainin fragment linked to the antimicrobial undecapeptide through an AGPA hinge. Moreover, since the presence of a KDEL unit or of tag54 did not influence significantly the biological activity, these moieties can be introduced when designing compounds to be retained in the endoplasmic reticulum and detected using a complementary epitope. These findings may contribute to the design of peptides to be expressed in plants.

Indexed as

Antimicrobial Cationic PeptidesGenetic EngineeringOligopeptidesPlantsPlants, Genetically ModifiedTransformation, GeneticAntimicrobial Cationic Peptideslysyl-lysyl-leucyl-phenylalanyl-lysyl-lysyl-isoleucyl-leucyl-lysyl-tyrosyl-leucinamideOligopeptides

Identifiers

PMID24376887
PMCPMC3871672
OpenAlexW1995645104

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.