Dermaseptin, a Peptide Antibiotic, Stimulates Microbicidal Activities of Polymorphonuclear Leukocytes

Ammar, Belinda; Périanin, Axel; Mor, Amram; Sarfati, G.; Tissot, M.; Nicolas, Pierre; Giroud, Jean‐Paul; Roch-Arveiller, M

doi:10.1006/bbrc.1998.8879

Cited by 41 publications

(23 citation statements)

References 25 publications

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“…The minimal inhibitory concentrations obtained in the antibacterial tests shown in Table II are slightly higher than those reported in the literature (7)(8)(9)(10)(11). However, there is no reason to believe that DS 01 has comparatively lesser antimicrobial activity than other dermaseptins since there are no standards and the experimental conditions used in the tests were more severe (on the order of 10 7 colony forming units/ml and Mueller-Hinton medium).…”

Section: Discussioncontrasting

confidence: 57%

“…Antimicrobial peptides have been produced by a number of Gram-positive and Gram-negative bacteria for billions of years to hinder the proliferation of other microorganisms that are closely related or confined within the same ecological niche (1)(2)(3)(4)(5)(6). In vertebrates, these peptides are synthesized by lymphoid cells, granular epithelial cells of the skin, respiratory and urogenital tracts, and also by the gastrointestinal system (7)(8)(9)(10). A defense strategy against invading microorganisms is well documented in amphibians and consists of the biosynthesis of a large number of small polycationic peptides integrated with the cell-mediated immune system.…”

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confidence: 99%

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Dermaseptins from Phyllomedusa oreades andPhyllomedusa distincta

Brand¹,

Leite²,

Silva³

et al. 2002

Journal of Biological Chemistry

103

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Amphibian skin secretions are known as a rich source of biologically active molecules, most of which are alkaloids, biogenic amines, and peptides. Dermaseptins are a class of antimicrobial peptides present in tree frogs of the Phyllomedusa genus. They are cationic molecules of 28 -34 residues that permeabilize the membrane of Gram-positive and Gram-negative bacteria, yeasts, and filamentous fungi, showing little or no hemolytic activity. This work reports the isolation, molecular mass analysis, primary structure determination, biological activities, and potential therapeutic applications of an antimicrobial peptide found in the skin secretion of Phyllomedusa oreades, which is a newly described amphibian species endemic of the Brazilian savanna. DS 01 is a 29-residue-long peptide with a molecular mass of 2793.39 Da showing antibacterial properties against Gram-positive and Gram-negative bacteria in the range of 3-25 M. Anti-protozoan activity was investigated using T. cruzi in its trypomatigote and epimastigote forms cultivated in both cell culture and blood media. Within 2 h after incubation with DS 01 at a final concentration of ϳ6 M, no protozoan cells were detected. Two synthetic dermaseptins, described previously by our group and named dermadistinctins K and L (DD K and DD L), also had their anti-Trypanosoma cruzi activity investigated and demonstrated similar properties. Toxicity of DS 01 to mouse erythrocytes and white blood cells was evaluated by means of atomic force microscopy and flow cytometry. No morphological alterations were observed at a lytic concentration of DS 01, suggesting its therapeutic value especially as an anti-T. cruzi agent to prevent infections during blood transfusion.

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Section: Discussioncontrasting

confidence: 57%

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confidence: 99%

Dermaseptins from Phyllomedusa oreades andPhyllomedusa distincta

Brand¹,

Leite²,

Silva³

et al. 2002

Journal of Biological Chemistry

103

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“…Thus, the frog antimicrobial peptide dermaseptin S1 was shown to stimulate microbicidal activities of rat and human leukocytes (1), and more recently, the insectderived peptide CEMA (a cecropin-melittin hybrid) was reported to induce the expression of 35 genes in macrophages (27). Moreover, an increasing number of cationic peptides and proteins, including lactoferrin (3,22), bactericidal/permeability increasing protein (8), synthetic antiendotoxin peptides (7), dermaseptins (unpublished data), and CEMA (14), are reportedly endowed with lipopolysaccharide (LPS) binding activity.…”

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confidence: 99%

Antibacterial Properties of Dermaseptin S4 Derivatives with In Vivo Activity

Navon-Venezia

Feder

Gaidukov

et al. 2002

Antimicrob Agents Chemother

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135

100

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Staphylococcus aureus, Pseudomonas aeruginosa, and Escherichia coli were, respectively, 1 to 4, 1 to 4, and 1 to 16 g/ml. MICs of the short derivatives were rather similar or two to fourfold higher. Each of the three peptides was rapidly bactericidal in vitro, reducing the number of viable CFU of either E. coli or S. aureus by 6 log units in 30 min or less. Compared with MSI-78 or PG-1, K 4 -S4(1-13) was at least as potent against bacteria (assessed at two MIC multiples) but displayed lesser toxicity against human erythrocytes. Serial passage in subinhibitory concentrations led to emergence of resistance to commercial antibiotics but not to the L-or D isomer of either of the dermaseptin derivatives. The short derivatives were further investigated for antibacterial activity in vivo, using a peritonitis model of mice infected with P. aeruginosa. Naive mice in the vehicle control group exhibited 75% mortality, compared to 18 or 36% mortality in mice that received a single intraperitoneal injection (4.5 mg/kg) of K 4 -S4(1-16) or K 4 -S4(1-13), respectively. In vivo bactericidal activity was confirmed in neutropenic mice, where intraperitoneal administration of K 4 -S4(1-16) reduced the number of viable CFU in a dose-dependent manner by >3 log units within 1 h of exposure, and this was sustained for at least 5 h. Overall, the data suggest that dermaseptin S4 derivatives could be useful in treatment of infections, including infections caused by multidrug-resistant bacteria.

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“…However they present rapid and irreversible antimicrobial effect and no toxic effects in mammalian cells in vitro (Kustanovich et al, 2002;Navon-Venezia et al, 2002). In additiony to antimicrobial activity, some dermaseptins present other additional biological functions that have unclear relations with pathogen clearance, e.g., dermaseptin B2 (adenoregulin) stimulates the binding of agonists to A1 adenosine receptors and also enhances the binding of agonists to several G-protein coupled receptors in rat brain plasmatic membrane through a mechanism involving enhancement of guanyl nucleotide exchange at G-proteins (Shin et al, 1994); Dermaseptin-B4 stimulates insulin release by acute incubation with glucose-responsive cells (Marenah et al, 2004); Dermaseptin-S1 stimulates the production of reactive oxygen species and release of myeloperoxidase by polymorphonuclear leukocytes (Ammar et al, 1998). Gram-negative Salmonella typhimurium, wall-less Mycoplasma gallisepticum and M. mycoides show resistance to dermaseptin B9 from P. bicolor (Fleury et al, 1998).…”

Section: Frog Skin Active Peptides Family: Defence Against Pathogens mentioning

confidence: 99%