Ranatuerin 1T: an antimicrobial peptide isolated from the skin of the frog, Rana temporaria

Goraya, Jadvinder; Knoop, Floyd C.; Conlon, J. Michael

doi:10.1016/s0196-9781(98)00174-0

Cited by 22 publications

(12 citation statements)

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“…6, at least eight different peptide families produced in the skins of Ranid frogs may be recognized on the basis of amino‐acid sequence similarity. We propose that these families are named on the basis of the first member to have been discovered in each as follows: brevinin‐1 [15], which includes gaegurin‐5 and gaegurin‐6 [13] and ranatuerin‐4 [20]; brevinin‐2 [15], which includes rugosin A and B [14] and ranatuerin‐1T [22]; esculentin‐1 [18]; esculentin‐2 [16], which includes gaegurin‐4 [13] and rugosin C [14]; ranatuerin‐1 [20]; ranatuerin‐2 [20], which includes ranatuerin‐3 [20]; ranalexin [19]; and temporin [21], which includes peptides A1 and B9 [24] and ranatuerins 5, 6, 7, 8 and 9 [20]. The C‐terminal region of peptides of the brevinin‐1, ranalexin, brevinin‐2, esculentin‐1, esculetin‐2 and ranatuerin‐1 families contains a cystine‐bridged cyclic heptapeptide whereas the corresponding region of peptides of the ranatuerin‐2 family contains a cystine‐bridged cyclic hexapeptide.…”

Section: Discussionmentioning

confidence: 99%

“…Frogs from the genus Rana constitute an extremely diverse and widely distributed group, with an estimated 250 species world‐wide and at least 36 species having been identified in North America [12]. Analysis of skin secretions and/or skin extracts of different species of Ranid frogs has led to the characterization of gaegurins [13] and rugosins [14] from Rana rugosa , brevinins from Rana brevipoda porsa [15], Rana esculenta [16] and Rana sphenocephala [17], esculentins [18] from R. esculenta , ranalexin [19] and ranatuerins [20] from Rana catesbeiana , and temporins [21] and ranatuerin 1T [22] from Rana temporaria . Peptides of the brevinin family have also been isolated from an extract of gastric tissue from R. esculenta [23].…”

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confidence: 99%

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Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens

Goraya

Yuqi

et al. 2000

European Journal of Biochemistry

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The skins of frogs of the genus Rana synthesize a complex array of antimicrobial peptides that may be grouped into eight families on the basis of structural similarity. A total of 24 peptides with differential growth-inhibitory activity towards the Gram-positive bacterium Staphylococcus aureus, the Gram-negative bacterium Escherichia coli and the yeast Candida albicans were isolated from extracts of the skins of three closely related North American frogs, Rana luteiventris (spotted frog), Rana berlandieri (Rio Grande leopard frog) and Rana pipiens (Northern leopard frog). Structural characterization of the antimicrobial peptides demonstrated that they belonged to four of the known families: the brevinin-1 family, first identified in skin of the Asian frog Rana porosa brevipoda; the esculentin-2 family, first identified in the European frog Rana esculenta; the ranatuerin-2 family, first identified in the North American bullfrog Rana catesbeiana; and the temporin family, first identified in the European frog Rana temporaria. Peptides belonging to the brevinin-2, ranalexin, esculentin-1 and ranatuerin-1 families were not identified in the extracts. Despite the close phylogenetic relationship between the various species of Ranid frogs, the distribution and amino-acid sequences of the antimicrobial peptides produced by each species are highly variable and species-specific, suggesting that they may be valuable in taxonomic classification and molecular phylogenetic analysis.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens

Goraya

Yuqi

et al. 2000

European Journal of Biochemistry

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159

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“…It is becoming clear through many studies that antimicrobial peptides are an important component of the innate defenses of all species of life (3)(4)(5)(6)(7)(8). Antimicrobial peptides function by interacting with the cell membrane (1)(2)(3)(4)(5)(6).…”

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confidence: 99%

“…Several antimicrobial peptides such as magainin, a 23-residue antimicrobial peptide, have been successful in pharmaceutical and commercial development (5). Particularly, from the first discovery of bombinins in Bombina variegata (7), the skin of anurans (frogs and toads) has proven to be a rich source of peptides with a broad spectrum of antimicrobial activities (6,8,14). After the discovery of the magainins in 1987 (15), attention has been increasingly focused upon amphibian skin peptides as potential therapeutic agents (2,5,6).…”

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confidence: 99%

Systematic Peptide Engineering and Structural Characterization to Search for the Shortest Antimicrobial Peptide Analogue of Gaegurin 5

Won

Jung

Kim

et al. 2004

Journal of Biological Chemistry

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As part of an effort to develop new, low molecular mass peptide antibiotics, we searched for the shortest bioactive analogue of gaegurin 5 (GGN5), a 24-residue antimicrobial peptide. Thirty-one kinds of GGN5 analogues were synthesized, and their biological activities were analyzed against diverse microorganisms and human erythrocytes. The structural properties of the peptides in various solutions were characterized by spectroscopic methods. The N-terminal 13 residues of GGN5 were identified as the minimal requirement for biological activity. The helical stability, the amphipathic property, and the hydrophobic N terminus were characterized as the important structural factors driving the activity. To develop shorter antibiotic peptides, amino acid substitutions in an inactive 11-residue analogue were examined. Single tryptophanyl substitutions at certain positions yielded some active 11-residue analogues. The most effective site for the substitution was the hydrophobic-hydrophilic interface in the amphipathic helical structure. At this position, tryptophan was the most useful amino acid conferring favorable activity to the peptide. The introduced tryptophan played an important anchoring role for the membrane interaction of the peptides. Finally, two 11-residue analogues of GGN5, which exhibited strong bactericidal activity with little hemolytic activity, were obtained as property-optimized candidates for new peptide antibiotic development. Altogether, the present approach not only characterized some important factors for the antimicrobial activity but also provided useful information about peptide engineering to search for potent lead molecules for new peptide antibiotic development.Most organisms produce membrane-active peptides that exhibit antibiotic, fungicidal, hemolytic, virucidal, and tumoricidal activities (1, 2). It is becoming clear through many studies that antimicrobial peptides are an important component of the innate defenses of all species of life (3-8). Antimicrobial peptides function by interacting with the cell membrane (1-6). In particular, cationic, linear, helical peptides, which are the most well characterized group of antimicrobial peptides, function by the "barrel-stave" and/or "carpet-like" mechanism, leading to bacterial membrane permeation (1, 5, 9 -13). In membrane environments, the peptides generally adopt an amphipathic helical structure, positioning the hydrophobic residues on one side and the hydrophilic residues on the other side of the helical axis, whereas they assume a random coil conformation in aqueous solutions.Recently, antimicrobial peptides have become a potential source of new antibiotics to combat the increasing emergence of drug-resistant bacteria (4, 5). Several antimicrobial peptides such as magainin, a 23-residue antimicrobial peptide, have been successful in pharmaceutical and commercial development (5). Particularly, from the first discovery of bombinins in Bombina variegata (7), the skin of anurans (frogs and toads) has proven to be a rich source of peptides with ...

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“…Taxonomic identification of individual specimens is often difficult, especially in regions where several species coexist and produce hybrids. Analysis of skin secretions and skin extracts of species of different Ranid frogs has led to the characterization of gaegurins (12) and rugosins (13) from Rana rugosa , brevinins from Rana brevipoda porsa (14), pipinins from Rana pipiens (15) brevinins (16) and esculentins (16) from Rana esculenta , ranalexin (17) and ranatuerins (18) from Rana catesbeiana and temporins (19) and ranatuerin 1T (20) from Rana temporaria . These peptides are relatively short, amphipathic and helical and, except for the temporins, also contain a cystine‐bridged cyclic hexapeptide or heptapeptide region.…”

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confidence: 99%

Peptides with antimicrobial activity of the brevinin‐1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala

Conlon

Halverson

Dulka

et al. 1999

The Journal of Peptide Research

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Three peptides with growth-inhibitory activity towards the gram-negative bacterium Eschericia coli were isolated from electrically stimulated secretions from the skin of the southern leopard frog, Rana sphenocephala. Structural characterization demonstrated that the peptides [brevinin-1Sa, minimum inhibitory concentration (MIC) = 55 microM; brevinin-1Sb, MIC = 17 microM; brevinin-1Sc, MIC = 14 microM] represent new members of the brevinin-1 family of antimicrobial peptides, previously isolated from several other species of frogs of the genus Rana. Their high concentration in skin secretions and extreme variability in amino acid sequence suggest that the brevinin family of peptides may be of value as molecular markers for the identification and taxonomic classification of Ranid frogs.

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Ranatuerin 1T: an antimicrobial peptide isolated from the skin of the frog, Rana temporaria

Cited by 22 publications

References 25 publications

Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens

Peptides with antimicrobial activity from four different families isolated from the skins of the North American frogs Rana luteiventris, Rana berlandieri and Rana pipiens

Systematic Peptide Engineering and Structural Characterization to Search for the Shortest Antimicrobial Peptide Analogue of Gaegurin 5

Peptides with antimicrobial activity of the brevinin‐1 family isolated from skin secretions of the southern leopard frog, Rana sphenocephala

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