Evidence map›Paper›PMID 29566082›Full record

ArticlePloS one2018

A D-enantiomer of the antimicrobial peptide GL13K evades antimicrobial resistance in the Gram positive bacteria Enterococcus faecalis and Streptococcus gordonii.

Helmut Hirt, Jeffrey W Hall, Elliot Larson, Sven-Ulrik Gorr

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.0field-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

26 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. ApoE Mimetic Peptide COG1410 KillsAntibiotics (Basel, Switzerland) · 2024
    Article
  5. Article
  6. Anti-Infection of Oral Microorganisms from Herbal Medicine ofDrug design, development and therapy · 2024
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Interactions of two enantiomers of a designer antimicrobial peptide with structural components of the bacterial cell envelope.Journal of peptide science : an official publication of the European Peptide Society · 2022
    Article
  13. Article
  14. Article
  15. Harnessing biomolecules for bioinspired dental biomaterials.Journal of materials chemistry. B · 2020
    Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Helmut HirtDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, United States of America.
Jeffrey W HallDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, United States of America.ORCID 0000-0002-0214-4062
Elliot LarsonDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, United States of America.
Sven-Ulrik GorrDepartment of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, United States of America.ORCID 0000-0002-7855-4949
University of Minnesota · US

Funding

Antibacterial and anti-inflammatory activities of Parotid Secretory ProteinR01DE017989 · NIDCR · UNIVERSITY OF MINNESOTA · PI GORR, SVEN-ULRIK · 2010 to 2013
$1.4M
NIDCR NIH HHS R01 DE017989NIH HHS R01 DE017989NIH HHS T90 DE0227232
6 · The paper itself

Abstract

Antimicrobial peptides represent an alternative to traditional antibiotics that may be less susceptible to bacterial resistance mechanisms by directly attacking the bacterial cell membrane. However, bacteria have a variety of defense mechanisms that can prevent cationic antimicrobial peptides from reaching the cell membrane. The L- and D-enantiomers of the antimicrobial peptide GL13K were tested against the Gram-positive bacteria Enterococcus faecalis and Streptococcus gordonii to understand the role of bacterial proteases and cell wall modifications in bacterial resistance. GL13K was derived from the human salivary protein BPIFA2. Minimal inhibitory concentrations were determined by broth dilution and a serial assay used to determine bacterial resistance. Peptide degradation was determined in a bioassay utilizing a luminescent strain of Pseudomonas aeruginosa to detect peptide activity. Autolysis and D-alanylation-deficient strains of E. faecalis and S. gordonii were tested in autolysis assays and peptide activity assays. E. faecalis protease inactivated L-GL13K but not D-GL13K, whereas autolysis did not affect peptide activity. Indeed, the D-enantiomer appeared to kill the bacteria prior to initiation of autolysis. D-alanylation mutants were killed by L-GL13K whereas this modification did not affect killing by D-GL13K. The mutants regained resistance to L-GL13K whereas bacteria did not gain resistance to D-GL13K after repeated treatment with the peptides. D-alanylation affected the hydrophobicity of bacterial cells but hydrophobicity alone did not affect GL13K activity. D-GL13K evades two resistance mechanisms in Gram-positive bacteria without giving rise to substantial new resistance. D-GL13K exhibits attractive properties for further antibiotic development.

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesDrug Resistance, BacterialEnterococcus faecalisGram-Positive BacteriaGram-Positive Bacterial InfectionsIsomerismMicrobial Sensitivity TestsPeptide FragmentsStreptococcus gordoniiAnti-Infective AgentsAntimicrobial Cationic PeptidesPeptide Fragments

Identifiers

PMID29566082
PMCPMC5864073
OpenAlexW2792066431

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.