Evidence map›Paper›PMID 31356627›Full record

ArticlePloS one2019

Mode of action of the antimicrobial peptide Mel4 is independent of Staphylococcus aureus cell membrane permeability.

Muhammad Yasir, Debarun Dutta, Mark D P Willcox

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

61 citing papers in PubMed, 114 citations in OpenAlex.

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  13. The Role ofPharmaceutics · 2024
    Review
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  18. The activity of antimicrobial peptoids against multidrug-resistant ocular pathogens.Contact lens & anterior eye : the journal of the British Contact Lens Association · 2024
    Article
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  20. Review

1 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Muhammad YasirSchool of Optometry and Vision Science, University of New South Wales, Sydney, New South Wales, Australia.ORCID 0000-0003-4589-4311
Debarun DuttaSchool of Optometry and Vision Science, University of New South Wales, Sydney, New South Wales, Australia.
Mark D P WillcoxSchool of Optometry and Vision Science, University of New South Wales, Sydney, New South Wales, Australia.
UNSW Sydney · AUAston University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mel4 is a novel cationic peptide with potent activity against Gram-positive bacteria. The current study examined the anti-staphylococcal mechanism of action of Mel4 and its precursor peptide melimine. The interaction of peptides with lipoteichoic acid (LTA) and with the cytoplasmic membrane using DiSC(3)-5, Sytox green, Syto-9 and PI dyes were studied. Release of ATP and DNA/RNA from cells exposed to the peptides were determined. Bacteriolysis and autolysin-activated cell death were determined by measuring decreases in OD620nm and killing of Micrococcus lysodeikticus cells by cell-free media. Both peptides bound to LTA and rapidly dissipated the membrane potential (within 30 seconds) without affecting bacterial viability. Disturbance of the membrane potential was followed by the release of ATP (50% of total cellular ATP) by melimine and by Mel4 (20%) after 2 minutes exposure (p<0.001). Mel4 resulted in staphylococcal cells taking up PI with 3.9% cells predominantly stained after 150 min exposure, whereas melimine showed 34% staining. Unlike melimine, Mel4 did not release DNA/RNA. Cell-free media from Mel4 treated cells hydrolysed peptidoglycan and produced greater zones of inhibition against M. lysodeikticus lawn than melimine treated samples. These findings suggest that pore formation is unlikely to be involved in Mel4-mediated membrane destabilization for staphylococci, since there was no significant Mel4-induced PI staining and DNA/RNA leakage. It is likely that the S. aureus killing mechanism of Mel4 involves the release of autolysins followed by cell death. Whereas, membrane interaction is the primary bactericidal activity of melimine, which includes membrane depolarization, pore formation, release of cellular contents leading to cell death.

Indexed as

Antimicrobial Cationic PeptidesAnimalsCell MembraneDNA, BacterialHorsesLipopolysaccharidesMicrococcusRNA, BacterialStaphylococcus aureusTeichoic AcidsAntimicrobial Cationic PeptidesDNA, BacterialLipopolysaccharideslipoteichoic acidRNA, BacterialTeichoic Acids

Identifiers

PMID31356627
PMCPMC6663011
OpenAlexW2964809094

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.