Evidence map›Paper›PMID 16127062›Full record

ArticleAntimicrobial agents and chemotherapy2005

Structure-function characterization and optimization of a plant-derived antibacterial peptide.

Mougli Suarez, Marisa Haenni, Stéphane Canarelli, Florian Fisch, Pierre Chodanowski, Catherine Servis, Olivier Michielin, Ruth Freitag, Philippe Moreillon, Nicolas Mermod

Abstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Antibacterial effect ofOpen veterinary journal · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Frontiers in pharmacology · 2020
    Article
  12. Article
  13. Review
  14. Review
  15. Microbiological Assessment ofOpen access Macedonian journal of medical sciences · 2016
    Article
  16. Article
  17. 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

10 authors.

Mougli SuarezInstitute of Biotechnology, University of Lausanne, Switzerland.
Marisa Haenni
Stéphane Canarelli
Florian Fisch
Pierre Chodanowski
Catherine Servis
Olivier Michielin
Ruth Freitag
Philippe Moreillon
Nicolas Mermod

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crushed seeds of the Moringa oleifera tree have been used traditionally as natural flocculants to clarify drinking water. We previously showed that one of the seed peptides mediates both the sedimentation of suspended particles such as bacterial cells and a direct bactericidal activity, raising the possibility that the two activities might be related. In this study, the conformational modeling of the peptide was coupled to a functional analysis of synthetic derivatives. This indicated that partly overlapping structural determinants mediate the sedimentation and antibacterial activities. Sedimentation requires a positively charged, glutamine-rich portion of the peptide that aggregates bacterial cells. The bactericidal activity was localized to a sequence prone to form a helix-loop-helix structural motif. Amino acid substitution showed that the bactericidal activity requires hydrophobic proline residues within the protruding loop. Vital dye staining indicated that treatment with peptides containing this motif results in bacterial membrane damage. Assembly of multiple copies of this structural motif into a branched peptide enhanced antibacterial activity, since low concentrations effectively kill bacteria such as Pseudomonas aeruginosa and Streptococcus pyogenes without displaying a toxic effect on human red blood cells. This study thus identifies a synthetic peptide with potent antibacterial activity against specific human pathogens. It also suggests partly distinct molecular mechanisms for each activity. Sedimentation may result from coupled flocculation and coagulation effects, while the bactericidal activity would require bacterial membrane destabilization by a hydrophobic loop.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsBacteriaCell MembraneCulture MediaEscherichia coliFungiHemolysisHumansIn Vitro TechniquesMass SpectrometryMicrobial Sensitivity TestsMicroscopy, ConfocalModels, StructuralMolecular Sequence DataMoringaAnti-Bacterial AgentsCulture MediaPeptides

Identifiers

PMID16127062
PMCPMC1195432

What OpenQuestion holds

Textmetadata
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.