Studies of the mechanism of an antibacterial peptide (cecropinA–magainin) on methicillin‐resistant <i>Staphylococcus aureus</i> membranes

Yu, Longmei; Zhu, Mingzhao; Liu, Erqiang; Yang, Tianen; Chen, Xiangjun; Wang, Xiuqing

doi:10.1002/bab.1429

Cited by 8 publications

(3 citation statements)

References 18 publications

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“…The same conclusion has been obtained in the case of CecXJ-37 N, a cationic peptide similar to cecropin, demonstrating that the peptide induced pore-formation, morphological changes and lysed E. coli cells [ 52 ]. In addition, other authors reported the capacity of a cecropin A-magainin hybride peptide to destroy the integrity of the bacterial cell membrane [ 53 ].…”

Section: Discussionmentioning

confidence: 99%

Lysozyme enhances the bactericidal effect of BP100 peptide against Erwinia amylovora, the causal agent of fire blight of rosaceous plants

Cabrefiga

Seguí

2017

BMC Microbiol

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BackgroundFire blight is an important disease affecting rosaceous plants. The causal agent is the bacteria Erwinia amylovora which is poorly controlled with the use of conventional bactericides and biopesticides. Antimicrobial peptides (AMPs) have been proposed as a new compounds suitable for plant disease control. BP100, a synthetic linear undecapeptide (KKLFKKILKYL-NH2), has been reported to be effective against E. amylovora infections. Moreover, BP100 showed bacteriolytic activity, moderate susceptibility to protease degradation and low toxicity. However, the peptide concentration required for an effective control of infections in planta is too high due to some inactivation by tissue components. This is a limitation beause of the high cost of synthesis of this compound. We expected that the combination of BP100 with lysozyme may produce a synergistic effect, enhancing its activity and reducing the effective concentration needed for fire blight control.ResultsThe combination of a synhetic multifunctional undecapeptide (BP100) with lysozyme produces a synergistic effect. We showed a significant increase of the antimicrobial activity against E. amylovora that was associated to the increase of cell membrane damage and to the reduction of cell metabolism. Combination of BP100 with lysozyme reduced the time required to achieve cell death and the minimal inhibitory concentration (MIC), and increased the activity of BP100 in the presence of leaf extracts even when the peptide was applied at low doses. The results obtained in vitro were confirmed in leaf infection bioassays.ConclusionsThe combination of BP100 with lysozyme showed synergism on the bactericidal activity against E. amylovora and provide the basis for developing better formulations of antibacterial peptides for plant protection.

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Section: Discussionmentioning

confidence: 99%

Lysozyme enhances the bactericidal effect of BP100 peptide against Erwinia amylovora, the causal agent of fire blight of rosaceous plants

Cabrefiga

Seguí

2017

BMC Microbiol

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“…The bacterial density was then adjusted to 10 8 CFU mL À1 with Z buffer (0.29 g of Na 2 HPO 4 Á12H 2 O, 0.8 g of NaCl, 0.024 g of KH 2 PO 4 , 0.02 g of KCl, 0.025 g of MgSO 4 and 0.39 g of 2-hydroxy-1-ethanethiol per 100 mL), and the suspension was mixed with 100 lL of an RSS solution (6.3%) and 100 lL of 2-nitrophenyl b-D-galactopyranoside (ONPG; 1 mg mL À1 ) with heating in a water bath at 37°C for 0, 1, 2, 3, 4 and 5 h, followed by the measurement of OD 405 using a TU-1900 spectrophotometer (Beijing General Instrument, China). A Triton X-100 solution was used as a positive control, and PBS was used as a negative control (Yu et al, 2016).…”

Section: Measurement Of the Cytoplasmic Membrane Permeabilitymentioning

confidence: 99%

Antimicrobial activity of Arg–Ser–Ser against the food‐borne pathogen Pseudomonas aeruginosa

Liu

Brennan

et al. 2019

Int J of Food Sci Tech

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We had previously reported a peptide sequence, Arg-Ser-Ser (RSS), which was identified after coincubation of an edible orchid species, Dendrobium aphyllum, with Lactobacillus amylolyticus. In this study, we investigated the potential mechanism of the antibacterial effect of RSS on the pathogen Pseudomonas aeruginosa. The minimum inhibitory concentration of RSS for P. aeruginosa was 6.3%, and the peptide was shown to induce morphological damage to bacterial cells. RSS treatment increased the cell surface zeta potential, hydrophobicity and cell membrane permeability, indicating that the positively charged RSS likely interacted with the negatively charged bacterial membrane. Moreover, leakage of potassium ions and proteins from bacterial cells was increased by RSS by 30 ppm and 13.5 lg mL À1 , respectively. In conclusion, RSS treatment caused leakage of cellular components from P. aeruginosa cells, mainly through damaging the cell membrane by electrostatic action. Thus, RSS may be a potent new antimicrobial agent.

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“…The purpose of the present study was to gain further insight into the interaction between colistin and bacterial cells including its underlying mechanism of action. Cytoplasmic membrane damage was assessed by measuring potassium loss from colistin-treated cells, as leakage of this intracellular solute is an early sign that membrane integrity has been compromised (Yu et al 2016 ; Liang et al 2016 ). Colistin-treated bacteria were also examined by flow cytometry and scanning electron microscopy (SEM) as changes in the size and shape of cells can be useful in identifying antibiotic targets too (Peach et al 2013 ; Cushnie et al 2016 ).…”

Section: Introductionmentioning

confidence: 99%

Colistin causes profound morphological alteration but minimal cytoplasmic membrane perforation in populations of Escherichia coli and Pseudomonas aeruginosa

et al. 2018

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Whilst colistin (polymyxin E) represents the last mainstream treatment option for multidrug-resistant Gram-negative pathogens, details of its mechanism of action remain to be fully resolved. In this study, the effects of sub-inhibitory, inhibitory-bactericidal, and supra-bactericidal levels of colistin on the membrane integrity and morphology of Escherichia coli and Pseudomonas aeruginosa were investigated using potassium loss, flow cytometry, and scanning electron microscopy (SEM). Supra-bactericidal colistin concentrations induced just 4–12% intracellular potassium loss from bacteria after 24 h. Flow cytometry data suggested colistin might alter cell arrangement, and SEM confirmed the antibiotic causes bacterial aggregation. Filamentation was not detected in either species at any concentration or time-point up to 24 h. These results argue against the hypotheses that colistin kills bacteria by puncturing the cytoplasmic membrane or disrupting DNA synthesis. The colistin-induced bacterial aggregation detected has implications for the interpretation of MBC, time-kill, and other test results obtained with this antibiotic.Electronic supplementary materialThe online version of this article (10.1007/s00203-018-1485-3) contains supplementary material, which is available to authorized users.

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Studies of the mechanism of an antibacterial peptide (cecropinA–magainin) on methicillin‐resistant Staphylococcus aureus membranes

Cited by 8 publications

References 18 publications

Lysozyme enhances the bactericidal effect of BP100 peptide against Erwinia amylovora, the causal agent of fire blight of rosaceous plants

Lysozyme enhances the bactericidal effect of BP100 peptide against Erwinia amylovora, the causal agent of fire blight of rosaceous plants

Antimicrobial activity of Arg–Ser–Ser against the food‐borne pathogen Pseudomonas aeruginosa

Colistin causes profound morphological alteration but minimal cytoplasmic membrane perforation in populations of Escherichia coli and Pseudomonas aeruginosa

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