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2001
Lamberty M, Zachary Daniel, Lanot R, Bordereau C, Robert A, Hoffmann Jules A, Bulet Philippe
Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect. Article de journal
Dans: J. Biol. Chem., vol. 276, non 6, p. 4085–4092, 2001, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Anti-Bacterial Agents, Antifungal Agents, Base Sequence, Chromatography, Cysteine, DNA Primers, High Pressure Liquid, hoffmann, Immunohistochemistry, Isoptera, M3i, Peptides, Protein Conformation, Recombinant Proteins, Sequence Homology
@article{lamberty_insect_2001,
title = {Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect.},
author = {M Lamberty and Daniel Zachary and R Lanot and C Bordereau and A Robert and Jules A Hoffmann and Philippe Bulet},
doi = {10.1074/jbc.M002998200},
issn = {0021-9258},
year = {2001},
date = {2001-02-01},
journal = {J. Biol. Chem.},
volume = {276},
number = {6},
pages = {4085--4092},
abstract = {Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively present in hemocyte granules and in salivary glands. The presence of termicin and spinigerin in unchallenged termites contrasts with observations in evolutionary recent insects or insects undergoing complete metamorphosis, in which antimicrobial peptides are induced in the fat body and released into the hemolymph after septic injury.},
keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Antifungal Agents, Base Sequence, Chromatography, Cysteine, DNA Primers, High Pressure Liquid, hoffmann, Immunohistochemistry, Isoptera, M3i, Peptides, Protein Conformation, Recombinant Proteins, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively present in hemocyte granules and in salivary glands. The presence of termicin and spinigerin in unchallenged termites contrasts with observations in evolutionary recent insects or insects undergoing complete metamorphosis, in which antimicrobial peptides are induced in the fat body and released into the hemolymph after septic injury.
1996
Ehret-Sabatier L, Loew D, Goyffon M, Fehlbaum P, Hoffmann Jules A, van Dorsselaer A, Bulet Philippe
Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood Article de journal
Dans: J. Biol. Chem., vol. 271, non 47, p. 29537–29544, 1996, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Chromatography, Cysteine, Electron, Hemolymph, Hemolysis, High Pressure Liquid, hoffmann, M3i, Mass Spectrometry, Microscopy, Peptides, Scorpions
@article{ehret-sabatier_characterization_1996,
title = {Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood},
author = {L Ehret-Sabatier and D Loew and M Goyffon and P Fehlbaum and Jules A Hoffmann and A van Dorsselaer and Philippe Bulet},
issn = {0021-9258},
year = {1996},
date = {1996-11-01},
journal = {J. Biol. Chem.},
volume = {271},
number = {47},
pages = {29537--29544},
abstract = {We have isolated, from the hemolymph of unchallenged scorpions of the species Androctonus australis, three distinct antimicrobial peptides, which we have fully characterized by Edman degradation, electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization mass spectrometry. Two are novel molecules: (i) androctonin, a 25-residue peptide with two disulfide bridges, active against both bacteria (Gram-positive and Gram-negative) and fungi and showing marked sequence homology to tachyplesins and polyphemusins from horseshoe crabs; and (ii) buthinin, a 34-residue antibacterial (Gram-positive and Gram-negative) peptide with three disulfide bridges. The third peptide contains 37 residues and three disulfide bridges and clearly belongs to the family of anti-Gram-positive insect defensins. We have synthesized androctonin and explored its activity spectrum and mode of action.},
keywords = {Animals, Anti-Bacterial Agents, Chromatography, Cysteine, Electron, Hemolymph, Hemolysis, High Pressure Liquid, hoffmann, M3i, Mass Spectrometry, Microscopy, Peptides, Scorpions},
pubstate = {published},
tppubtype = {article}
}
We have isolated, from the hemolymph of unchallenged scorpions of the species Androctonus australis, three distinct antimicrobial peptides, which we have fully characterized by Edman degradation, electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization mass spectrometry. Two are novel molecules: (i) androctonin, a 25-residue peptide with two disulfide bridges, active against both bacteria (Gram-positive and Gram-negative) and fungi and showing marked sequence homology to tachyplesins and polyphemusins from horseshoe crabs; and (ii) buthinin, a 34-residue antibacterial (Gram-positive and Gram-negative) peptide with three disulfide bridges. The third peptide contains 37 residues and three disulfide bridges and clearly belongs to the family of anti-Gram-positive insect defensins. We have synthesized androctonin and explored its activity spectrum and mode of action.
Charlet Maurice, Chernysh S, Philippe H, Hetru Charles, Hoffmann Jules A, Bulet Philippe
Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis Article de journal
Dans: J. Biol. Chem., vol. 271, non 36, p. 21808–21813, 1996, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology
@article{charlet_innate_1996,
title = {Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis},
author = {Maurice Charlet and S Chernysh and H Philippe and Charles Hetru and Jules A Hoffmann and Philippe Bulet},
issn = {0021-9258},
year = {1996},
date = {1996-09-01},
journal = {J. Biol. Chem.},
volume = {271},
number = {36},
pages = {21808--21813},
abstract = {We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.},
keywords = {Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.
