Antimicrobial peptide from the skin secretion of the frog Leptodactylus syphax (original) (raw)
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Molecules, 2018
Amphibians´ skin produces a diverse array of antimicrobial peptides that play a crucial role as the first line of defense against microbial invasion. Despite the immense richness of wild amphibians in Argentina, current knowledge about the presence of peptides with antimicrobial properties is limited to a only few species. Here we used LC-MS-MS to identify antimicrobial peptides with masses ranging from 1000 to 4000 Da from samples of skin secretions of Leptodactylus latrans (Anura: Leptodactylidae). Three novel amino acid sequences were selected for chemical synthesis and further studies. The three synthetic peptides, named P1-Ll-1577, P2-Ll-1298, and P3-Ll-2085, inhibited the growth of two ATCC strains, namely Escherichia coli and Staphylococcus aureus. P3-Ll-2085 was the most active peptide. In the presence of trifluoroethanol (TFE) and anionic liposomes, it adopted an amphipathic α-helical structure. P2-Ll-1298 showed slightly lower activity than P3-Ll-2085. Comparison of the MI...
Biochimica Et Biophysica Acta-protein Structure and Molecular Enzymology, 2001
Seven peptides (XT-1^XT-7) with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of the diploid clawed frog, Xenopus tropicalis. Structural characterization of the peptides demonstrated that amino acid sequence similarity to antimicrobial peptides previously isolated from Xenopus laevis was low, suggesting that the species are not closely related phylogenetically. Peptides XT-5 and XT-3 are probably the orthologs of X. laevis peptide glycine-leucine amide (PGL a ) and the N-terminal spacer region of prolevitide, respectively. XT-1, XT-6 and XT-7 show limited structural similarity to the spacer region of X. laevis procaeruleins and the paralogs XT-2 and XT-4 are similar to corresponding regions of proxenopsin. Orthologs of the magainins were not identified. The C-terminally K-amidated peptide XT-7 (GLLGPLLKIAAKVGSNLL.NH 2 ) showed the lowest minimum inhibitory concentrations against reference microorganisms (Staphylococcus aureus 5 WM, Escherichia coli 5 WM, and Candida albicans 40 WM) and was also active against clinical isolates of methicillin-resistant S. aureus, Staphylococcus epidermidis, Staphylococcus saprophyticus, Streptococcus group C, Shigella sonnei, Pseudomonas aeruginosa and Enterobacter cloacae. The peptide was, however, hemolytic against human erythrocytes (50% lysis at 70 WM). Circular dichroism studies showed that XT-7 has a random structure in aqueous solution, pH 7.0 but adopts an K-helical conformation in the presence of 50% trifluoroethanol. Decreasing the cationicity of XT-7 either by replacement of the C-terminal CONH 2 group by COOH or by deletion of the Lys 8 residue produced analogs with greatly ( s 10-fold) decreased antimicrobial potencies. ß
Novel Antimicrobial Peptides Isolated from Skin Secretions of the Mexican Frog Hyla eximia
Protein and Peptide Letters, 2009
High-resolution mass spectrometry-based peptidomics has been used to characterize several components in electro-stimulated skin secretions of the endemic Mexican frog Pachymedusa dacnicolor. Peptide mass screening performed in an Orbitrap-XL mass spectrometer showed that P. dacnicolor skin secretions possess 194 different components with molecular masses ranging mainly from 500 to 6,000 Da. Dozens of molecules were partially sequenced including two novel protease inhibitors. Additionally, one posttranslationally modified bradykinin and two novel dermaseptin-like antimicrobial peptides were fully sequenced. The novel peptide named here DMS-DA5 was fully characterized and showed potent antibacterial activity against various bacteria such as Escherichia coli, Bacillus subtilis, Salmonella enterica serovar typhimurium, and Pseudomonas aeruginosa with minimal inhibitory concentrations from 3.10 to 25.0 lM.
Toxicon : official journal of the International Society on Toxinology, 2008
Peptidomic analysis of norepinephrine-stimulated skin secretions from Hose's rock frog Odorrana hosii (Boulenger, 1891) led to the isolation of 8 peptides with differential antibacterial activities. Structural characterization demonstrated that the peptides belonged to the esculentin-1 (1 peptide), esculentin-2 (1 peptide), brevinin-1 (2 peptides), brevinin-2 (2 peptides), and nigrocin-2 (2 peptides) families of antimicrobial peptides. Similar analysis of skin secretions from the Malaysian fire frog Hylarana picturata (Boulenger, 1920) led to the isolation and characterization of peptides belonging to the brevinin-1 (2 peptides), brevinin-2 (5 peptides), and temporin (1 peptide) families. The differences in antimicrobial activities of paralogous peptides provide insight into structure-activity relationships, emphasizing the importance of cationicity in determining potency. The substitution Lys11-->Gln in brevinin-1HSa (FLPAVLRVAAKIVPTVFCAISKKC) from O. hosii abolishes growth...
Peptides, 2010
Peptidomic analysis of norepinephrine-stimulated skin secretions of the South-East Asian frog Hylarana erythraea (formerly Rana erythraea partim) has led to the identification of multiple peptides with antimicrobial activity. Structural characterization of the peptides demonstrated that they belong to the brevinin-1 (3), brevinin-2 (2), esculentin-2 (4), and temporin (1) families. The values in parentheses indicate the number of paralogs. In addition, a peptide (GVIKSVLKGVAKTVALG ML.NH(2)) was isolated that shows some structural similarity to the brevinin-2-related peptides (B2RP) previously isolated from North American frogs of the genus Lithobates. A synthetic replicate of the species B2RP showed broad-spectrum growth inhibitory activity against reference strains of Escherichia coli (MIC=12.5 microM), Staphylococcus aureus (MIC=12.5 microM) and Candida albicans (MIC=50 microM) and was active against multidrug-resistant clinical isolates of Acetinobacter baumannii (MIC in the range...
Comparative Biochemistry and Physiology C-toxicology & Pharmacology, 2011
Five peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus clivii Peracca, 1898 (Pipidae). Characterization of the peptides demonstrated that they are structurally similar to magainins (2 peptides), caerulein-precursor fragments, CPF (2 peptides), and xenopsin-precursor fragments, XPF (1 peptide) that have been previously isolated from other species of the genus Xenopus. The magainins and the XPF peptide were active only against the Gram-negative microorganism Escherichia coli whereas the CPF peptides were also active against the Gram-positive Staphylococcus aureus. The most abundant antimicrobial peptide in the secretions, CPF-C1 (GFGSLLGKALRLG ANVL.NH 2 ) inhibited the growth of the Gram-negative bacteria Acinetobacter baumannii, Klebsiella pneumoniae, and Pseudomonas aeruginosa (MIC ≤ 25 μM) suggesting potential for development into an antiinfective agent for use against these emerging antibiotic-resistant pathogens.
Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta
FEBS Letters, 1993
Three antimicrobial peptides were isolated from skin secretion of the European frog. Rana esculentu. Two of them show similarity to brevinm-1 and brevinm-2. respectively. two antimrcrobial peptides recently isolated from a Japanese frog [Mortkawa. N., Hagiwara, K. and Nakajima. T. (1992) Biochem. Biophys. Res. Commun 189. 1841901. The third one, named esculentin, is 46 residues long and represents a different type of peptide. All these peptides have as a common motif an intramolecular dtsulfide bridge located at the COOH-terminal end. The peptides from R. esculentn show dtstmctive antibacterial activity against representative Gram-negative and Gram-posmve bacterial species. In parttcular, esculentm is the most active against Staphylococcus aureus. and has a much lower hemolytic activity.
International Journal of Peptide Research and Therapeutics, 2011
In this study, we extracted and purified antimicrobial peptides (AMPs) secreted from skin of Euphlyctis cyanophlyctis using reverse phase-high performance liquid chromatography. Three AMPs were isolated from skin secretions of this frog and sequenced using tandem mass spectrometry. The purified peptides were named buforin-EC (1875.05 ± 0.5 Da), cyanophlyctin (2347.50 ± 0.5 Da) and temporin-ECa (1013.33 ± 0.5 Da). Multiple alignments and homology search showed that buforin-EC, cyanophlyctin and temporin-ECa had a homology of 71.43, 47.1, and 69.23% to buforin II, brevinin-2EC, and temporin-1CSc, respectively. Antimicrobial tests demonstrated that our peptides have a great antimicrobial effect on both grampositive and gram-negative bacteria. The results indicated that they have an overall minimum inhibitory concentration (MIC) below 13 lM against E. coli. No hemolysis was observed in around of their MIC values. In conclusion, skin secretions of E. cyanophlyctis contain a novel class of AMPs with the proper characteristics.
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2009
The skins of amphibians secrete small antimicrobial peptides that fight infection and are being explored as potential alternatives to conventional antibiotics. In this study we combined mass spectrometry with cDNA sequencing to examine antimicrobial peptides in skin secretions from the Chinese frog Rana dybowskii. Thirteen peptides having precursor sequences that resemble known antimicrobial peptides from this genus were identified, ten of which were members of previously described peptide families based on their primary structures; i.e., brevinin-1, Japonicin-1, brevinin-2 and temporin. The other three peptides from R. dybowskii, which were named dybowskin-1CDYa, dybowskin-2 CDYa and dybowskin-2CDYb, had different amino acid compositions and little sequence similarity to known antimicrobial peptides. The carboxyl terminus of dybowskin-1CDY lacked amidation and is therefore clearly distinct from temporin peptides, whereas dybowskin-2CDYa and dybowskin-2CDYb consisted of 18 amino acids and were rich in Arg residues. Chemically synthesized peptides corresponding to mature dybowskin-1CDYa and dybowskin-2CDYa had strong antimicrobial activity and caused little hemolysis of human erythrocytes, suggesting they may serve as interesting templates for the development of novel antibiotics.