Les peptides de la défense antimicrobienne des vertébrés

Nicolas, P.; Mor, Amram; Delfour, Antoine

doi:10.4267/10608/3158

Cited by 9 publications

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“…It was recently recognized that in addition to the highly specific cell-mediated immune system, vertebrates are endowed for that purpose with an additional chemical defense system composed of antimicrobial peptides analogous to those found in invertebrates (Boman and Haltmark, 1987;Lehrer et al, 1991;Nicolas et al, 1992). This cell-free defense system provides vertebrates with small-sized peptides that are promptly synthesized upon induction, easily stored in large amounts and readily available for antimicrobial activity.…”

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Isolation and structure of novel defensive peptides from frog skin

Mor

Nicolas

1994

European Journal of Biochemistry

179

115

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In addition to the highly specific cell-mediated immune system, vertebrates possess an efficient host-defense mechanism against invading microorganisms which involves the synthesis of highly potent antimicrobial peptides with a large spectrum of activity. A 34-residue cationic and amphiphatic peptide, designated dermaseptin I, was recently isolated from the skin of the arboreal frog Phyllomedusa sauvugii and was shown to exhibit microbicidal activity against various pathogenic microorganisms including bacteria, yeast, protozoa and filamentous fungi. In this study, we report the isolation and characterization of four novel antimicrobial peptides from frog skin through the combined use of an anti-dermaseptin enzyme immunoassay and an antifungal bioassay. The 28-34-residue antimicrobial peptides are cationic, containing 3 -5 lysine residues that punctuate an alternating hydrophobic and hydrophilic sequence. Based on their primary structure, all four peptides can be fitted to a class L amphipathic a helix which places all lysine residues on the polar side of the helix. The four antimicrobial peptides have high sequence similarity with dermaseptin I (53 -94% similarity) suggesting that their respective genes are all members of the same family. In addition, pairwise sequence alignment of dermaseptin I and adenoregulin, a 33-residue cationic peptide recently isolated from frog skin and shown to enhance the binding of agonists to the A1 adenosine receptor, reveals 62% similarity (39% amino acid positional identity). Both peptides share a similar but non-identical spectrum of antimicrobial activity, being active against bacteria, yeast and filamentous molds. However, no significant hemolytic activity was found for these peptides which suggests a selectivity for prokaryotic cells. These findings indicate that adenoregulin should be included in the dermaseptin family of peptides. In addition, tryptic digestion of purified pro-dermaseptin I liberated a 15-amino-acid peptide identified as the authentic C-terminus of dermaseptin I. These results are in accordance with the predicted sequences of pro-dermaseptins obtained through molecular cloning, in which the dermaseptin progenitor sequences are located at the extreme C-terminus of the precursors.

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Isolation and structure of novel defensive peptides from frog skin

Mor

Nicolas

1994

European Journal of Biochemistry

179

115

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“…Ainsi, la panoplie de peptides antimicrobiens présents chez les invertébrés constitue un élé-ment majeur de l'immunité innée [21,22]. Des peptides semblables sont également présents chez les vertébrés, telle la défensine [23]. Ces peptides paraissent donc bien adaptés pour offrir une première ligne de défense efficace contre les agents infectieux.…”

Section: ] La Pro-enképhaline Engendre Par Un Processus De Maturatiounclassified

Peptides opioïdes, substances opiacées et réponse immunitaire.

Lefebvre¹,

Tasiemski²,

Salzet³

2000

Med Sci (Paris)

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“…(2). These peptides generally belong to families of biologically active peptides, which have their counterparts in mammals, such as tachykinins (3, 4), bradykinins (5, 6), angiotensin (7), caerulein/cholecystokinin (8), bombesin/gastrin-releasing peptide (9), opioid peptides (10), antimicrobial peptides (11,12), and hypophysiotropic neuropeptides (13,14). Although the physiological role of the various peptides synthesized and released by dermatous granular glands remains largely unknown, most of these peptides are produced in such enormous quantities that it is often possible to isolate enough material from a single skin to determine the amino acid sequence (15,16).…”

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Skin peptide tyrosine-tyrosine, a member of the pancreatic polypeptide family: isolation, structure, synthesis, and endocrine activity.

Mor

Chartrel

Vaudry

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Pancreatic polypeptide, peptide tyrosinetyrosine (PYY), and neuropeptide tyrosine (NPY), three members of a family of structurally related peptides, are mainly expressed in the endocrine pancreas, in endocrine cells of the gut, and in the brain, respectively. In the present study, we have isolated a peptide of the pancreatic polypeptide family from the skin of the South American arboreal frg Phylomedusa bicolor. The primary structure of the peptide was established as Tyr-Pro-Pro-Lys-Pro-Glu-Ser-Pro-Gly-Glu'O-AspAla-Ser-Pro-Glu-Glu-Met-Asn-Lys-Tyr2O-Leu-Thr-Ala-LeuArg-His-Tyr-Be-Asn-Leu3O-Val-Thr-Arg-Gln-Arg-Tyr-NH2. (2). These peptides generally belong to families of biologically active peptides, which have their counterparts in mammals, such as tachykinins (3, 4), bradykinins (5, 6), angiotensin (7), caerulein/cholecystokinin (8), bombesin/gastrin-releasing peptide (9), opioid peptides (10), antimicrobial peptides (11,12), and hypophysiotropic neuropeptides (13,14). Although the physiological role of the various peptides synthesized and released by dermatous granular glands remains largely unknown, most of these peptides are produced in such enormous quantities that it is often possible to isolate enough material from a single skin to determine the amino acid sequence (15,16).The pancreatic polypeptide (PP) family consists of three members of structurally related peptides, which all possess 36 amino acid residues, exhibit a C-terminal tyrosine amide moiety, and share common features of tertiary structure: (i) PP, originally discovered in the chicken pancreas (17), is exclusively localized in endocrine cells of pancreatic islets (18); (ii) peptide tyrosine-tyrosine (PYY), initially isolated from pig intestine (19), is primarily synthesized in gut endocrine cells (20) as well as in brainstem neurons (18) (23)(24)(25)(26)(27)(28)(29), suggesting that the genes encoding these two peptides arose from early duplication of an ancestral gene (30). In contrast, PP-like peptide is absent in fish and, therefore, it has been proposed that the PP gene arose from duplication of the PYY gene at the time of emergence of amphibians (30). The primary structures of all three members of the PP family have recently been determined in the frogs Rana catesbeiana (31) and Rana ridibunda (32, 33). However, the occurrence of PP-related peptides has never been reported in the skin of amphibians.We have recently undertaken the purification of a series of unusual polypeptides from the skin of the frog Phyllomedusa bicolor, using their antifungal activity as a biological test (34,35). We report here the isolation, characterization, and total synthesis of a 36-residue polypeptide, which shows 94% identity with R. ridibunda PYY (33). We also show that the synthetic replicate inhibits melanotropin (a-melanocytestimulating hormone, a-MSH) release from frog pars intermedia in very much the same way as NPY (32,36,37). This peptide has been called skin peptide tyrosine-tyrosine (SPYY). MATERIALS AND METHODSPurification of SPYY from Frog S...

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Les peptides de la défense antimicrobienne des vertébrés

Abstract: Les peptides de la défense antimicrobienne des vertébrés

Cited by 9 publications

References 0 publications

Isolation and structure of novel defensive peptides from frog skin

Isolation and structure of novel defensive peptides from frog skin

Peptides opioïdes, substances opiacées et réponse immunitaire.

Skin peptide tyrosine-tyrosine, a member of the pancreatic polypeptide family: isolation, structure, synthesis, and endocrine activity.

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