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

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 Di...

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Bibliographic Details
Published in:PloS one 2019-07, Vol.14 (7), p.e0215703-e0215703
Main Authors: Yasir, Muhammad, Dutta, Debarun, Willcox, Mark D P
Format: Article
Language:English
Subjects:
Amino acids
Analysis
Animals
Antibiotics
Antimicrobial agents
Antimicrobial Cationic Peptides - chemical synthesis
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacokinetics
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial peptides
ATP
Autolysins
Bacteria
Bactericidal activity
Biochemistry
Biology and Life Sciences
Cell death
Cell Membrane - metabolism
Cell membranes
Cell permeability
Deoxyribonucleic acid
Depolarization
Destabilization
DNA
DNA, Bacterial - metabolism
EDTA
Energy dissipation
Exposure
Gram-positive bacteria
Horses
Lipopolysaccharides - metabolism
Lipoteichoic acid
Medicine and Health Sciences
Membrane permeability
Membrane potential
Methicillin
Micrococcus - metabolism
Mode of action
Mortality
Novels
Optometry
Organic acids
Peptides
Peptidoglycans
Permeability
Pore formation
Proteins
Research and Analysis Methods
Ribonucleic acid
Risk factors
RNA
RNA, Bacterial - metabolism
Staining
Staphylococcus aureus
Staphylococcus aureus - metabolism
Staphylococcus aureus infections
Staphylococcus infections
Teichoic Acids - metabolism
Viability
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Summary: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
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0215703