Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers

Saint, Nathalie; Cadiou, Hervé; Bessin, Yannick; Molle, Gérard

doi:10.1016/s0005-2736(02)00470-4

Cited by 57 publications

(57 citation statements)

References 39 publications

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“…Previous studies showed that the pleurocidin isolated from the winter flounder, which migrates from its habitat of brackish water (0.8% salinity) to seawater (3.3% salinity), was naturally resistant to high concentrations of salt (5,25). Importantly, the pleurocidin did not depend on high salt concentrations for killing activity (5,28). The evidence from our study suggests that IMB-2 retains a level of salinity resistance similar to that of its ancestor peptide.…”

Section: Vol 55 2011supporting

confidence: 53%

A Novel Target-Specific, Salt-Resistant Antimicrobial Peptide against the Cariogenic Pathogen Streptococcus mutans

Mai

Tian

Gallant

et al. 2011

Antimicrob Agents Chemother

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In this study, we constructed and evaluated a target-specific, salt-resistant antimicrobial peptide (AMP) that selectively targeted Streptococcus mutans, a leading cariogenic pathogen. The rationale for creating such a peptide was based on the addition of a targeting domain of S. mutans ComC signaling peptide pheromone (CSP) to a killing domain consisting of a portion of the marine-derived, broad-spectrum AMP pleurocidin to generate a target-specific AMP. Here, we report the results of our assessment of such fusion peptides against S. mutans and two closely related species. The results showed that nearly 95% of S. mutans cells lost viability following exposure to fusion peptide IMB-2 (5.65 M) for 15 min. In contrast, only 20% of S. sanguinis or S. gordonii cells were killed following the same exposure. Similar results were also observed in dual-species mixed cultures of S. mutans with S. sanguinis or S. gordonii. The peptide-guided killing was further confirmed in S. mutans biofilms and was shown to be dose dependent. An S. mutans mutant defective in the CSP receptor retained 60% survival following exposure to IMB-2, suggesting that the targeted peptide predominantly bound to the CSP receptor to mediate killing in the wild-type strain. Our work confirmed that IMB-2 retained its activity in the presence of physiological or higher salt concentrations. In particular, the fusion peptide showed a synergistic killing effect on S. mutans with a preventive dose of NaF. In addition, IMB-2 was relatively stable in the presence of saliva containing 1 mM EDTA and did not cause any hemolysis. We also found that replacement of serine-14 by histidine improved its activity at lower pH. Because of its effectiveness, salt resistance, and minimal toxicity to host cells, this novel target-specific peptide shows promise for future development as an anticaries agent.

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Section: Vol 55 2011supporting

confidence: 53%

A Novel Target-Specific, Salt-Resistant Antimicrobial Peptide against the Cariogenic Pathogen Streptococcus mutans

Mai

Tian

Gallant

et al. 2011

Antimicrob Agents Chemother

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“…Moronecidin is a 22-amino acid, linear, cationic peptide with an amphipathic, ␣-helical structure that exhibits a more potent, broader spectrum of bactericidal activity than hepcidin (5). Peptides like moronecidin are thought to aggregate and interact with negatively charged bacterial membrane components and to disrupt them by forming pores or solubilizing the membrane via a "detergent" effect (53)(54)(55). This direct membrane disruption is believed to kill the bacterium by creating osmotic imbalance and loss of cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

Bass Hepcidin Synthesis, Solution Structure, Antimicrobial Activities and Synergism, and in Vivo Hepatic Response to Bacterial Infections

Lauth

Babon

Stannard

et al. 2005

Journal of Biological Chemistry

182

114

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Bass hepcidin was purified from the gill of hybrid striped bass (Morone chrysops ؋ Morone saxatilis) based on antimicrobial activity against Escherichia coli. This 21-amino acid peptide has 8 cysteines engaged in 4 disulfide bonds and is very similar to human hepcidin, an antimicrobial peptide with iron regulatory properties. To gain insight into potential role(s) of bass hepcidin in innate immunity in fish, we synthesized the peptide, characterized its antimicrobial activities in vitro, determined its solution structure by NMR, and quantified hepatic gene expression in vivo following infection of bass with the fish pathogens, Streptococcus iniae or Aeromonas salmonicida. Its structure is very similar to that of human hepcidin, including the presence of an antiparallel ␤-sheet, a conserved disulfide-bonding pattern, and a rare vicinal disulfide bond. Synthetic bass hepcidin was active in vitro against Gram-negative pathogens and fungi but showed no activity against key Gram-positive pathogens and a single yeast strain tested. Hepcidin was non-hemolytic at microbicidal concentrations and had lower specific activity than moronecidin, a broad spectrum, amphipathic, ␣-helical, antimicrobial peptide constitutively expressed in bass gill tissue. Good synergism between the bacterial killing activities of hepcidin and moronecidin was observed in vitro. Hepcidin gene expression in bass liver increased significantly within hours of infection with Gram-positive (S. iniae) or Gram-negative (A. salmonicida) pathogens and was 4 -5 orders of magnitude above base-line 24 -48 h post-infection. Our results suggest that hepcidin plays a key role in the antimicrobial defenses of bass and that its functions are potentially conserved between fish and human.

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“…Pleurocidin was isolated from the winter flounder Pleuronectes americanus (Walbaum) in 1997 (9), and its activity has been under investigation by several research groups (13,20,21,23,28). Also, pleurocidin genes have been cloned, and their genetic organization has been described (8, 10; S. E. Douglas, A. Patrzykat, J. Pytyck, and J. W. Gallant, submitted for publication).…”

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confidence: 99%

Novel Antimicrobial Peptides Derived from Flatfish Genes

Patrzykat

Gallant

Seo

et al. 2003

Antimicrob Agents Chemother

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We report on the identification of active novel antimicrobials determined by screening both the genomic information and the mRNA transcripts from a number of different flatfish for sequences encoding antimicrobial peptides, predicting the sequences of active peptides from the genetic information, producing the predicted peptides chemically, and testing them for their activities. We amplified 35 sequences from various species of flatfish using primers whose sequences are based on conserved flanking regions of a known antimicrobial peptide from winter flounder, pleurocidin. We analyzed the sequences of the amplified products and predicted which sequences were likely to encode functional antimicrobial peptides on the basis of charge, hydrophobicity, relation to flanking sequences, and similarity to known active peptides. Twenty peptides were then produced synthetically and tested for their activities against gram-positive and gram-negative bacteria and the yeast Candida albicans. The most active peptide (with the carboxy-terminus amidated sequence GWRTLLKKAEVK TVGKLALKHYL, derived from American plaice) showed inhibitory activity over a concentration range of 1 to 8 g/ml against a test panel of pathogens, including the intrinsically antibiotic-resistant organism Pseudomonas aeruginosa, methicillin-resistant Staphylococcus aureus, and C. albicans. The methods described here will be useful for the identification of novel peptides with good antimicrobial activities.

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Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers

Cited by 57 publications

References 39 publications

A Novel Target-Specific, Salt-Resistant Antimicrobial Peptide against the Cariogenic Pathogen Streptococcus mutans

A Novel Target-Specific, Salt-Resistant Antimicrobial Peptide against the Cariogenic Pathogen Streptococcus mutans

Bass Hepcidin Synthesis, Solution Structure, Antimicrobial Activities and Synergism, and in Vivo Hepatic Response to Bacterial Infections

Novel Antimicrobial Peptides Derived from Flatfish Genes

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