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1994
Cociancich S, Dupont A, Hegy G, Lanot R, Holder F, Hetru Charles, Hoffmann Jules A, Bulet Philippe
Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus Article de journal
Dans: Biochem. J., vol. 300 ( Pt 2), p. 567–575, 1994, ISSN: 0264-6021.
Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Proteins, Chromatography, Defensins, Gas Chromatography-Mass Spectrometry, Gel, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, Hemolymph, hoffmann, Insect Proteins, M3i, Peptides, Sequence Homology
@article{cociancich_novel_1994,
title = {Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus},
author = {S Cociancich and A Dupont and G Hegy and R Lanot and F Holder and Charles Hetru and Jules A Hoffmann and Philippe Bulet},
issn = {0264-6021},
year = {1994},
date = {1994-06-01},
journal = {Biochem. J.},
volume = {300 ( Pt 2)},
pages = {567--575},
abstract = {Insects belonging to the recent orders of the endopterygote clade (Lepidoptera, Diptera, Hymenoptera and Coleoptera) respond to bacterial challenge by the rapid and transient synthesis of a battery of potent antibacterial peptides which are secreted into their haemolymph. Here we present the first report on inducible antibacterial molecules in the sap-sucking bug Pyrrhocoris apterus, a representative species of the Hemiptera, which predated the Endoptergotes by at least 50 million years in evolution. We have isolated and characterized from immune blood of this species three novel peptides or polypeptides: (i) a 43-residue cysteine-rich anti-(Gram-positive bacteria) peptide which is a new member of the family of insect defensins; (ii) a 20-residue proline-rich peptide carrying an O-glycosylated substitution (N-acetylgalactosamine), active against Gram-negative bacteria; (iii) a 133-residue glycine-rich polypeptide also active against Gram-negative bacteria. The proline-rich peptide shows high sequence similarities with drosocin, an O-glycosylated antibacterial peptide from Drosophila, and also with the N-terminal domain of diptericin, an inducible 9 kDa antibacterial peptide from members of the order Diptera, whereas the glycine-rich peptide has similarities with the glycine-rich domain of diptericin. We discuss the evolutionary aspects of these findings.},
keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Blood Proteins, Chromatography, Defensins, Gas Chromatography-Mass Spectrometry, Gel, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, Hemolymph, hoffmann, Insect Proteins, M3i, Peptides, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Insects belonging to the recent orders of the endopterygote clade (Lepidoptera, Diptera, Hymenoptera and Coleoptera) respond to bacterial challenge by the rapid and transient synthesis of a battery of potent antibacterial peptides which are secreted into their haemolymph. Here we present the first report on inducible antibacterial molecules in the sap-sucking bug Pyrrhocoris apterus, a representative species of the Hemiptera, which predated the Endoptergotes by at least 50 million years in evolution. We have isolated and characterized from immune blood of this species three novel peptides or polypeptides: (i) a 43-residue cysteine-rich anti-(Gram-positive bacteria) peptide which is a new member of the family of insect defensins; (ii) a 20-residue proline-rich peptide carrying an O-glycosylated substitution (N-acetylgalactosamine), active against Gram-negative bacteria; (iii) a 133-residue glycine-rich polypeptide also active against Gram-negative bacteria. The proline-rich peptide shows high sequence similarities with drosocin, an O-glycosylated antibacterial peptide from Drosophila, and also with the N-terminal domain of diptericin, an inducible 9 kDa antibacterial peptide from members of the order Diptera, whereas the glycine-rich peptide has similarities with the glycine-rich domain of diptericin. We discuss the evolutionary aspects of these findings.
1993
Bulet Philippe, Dimarcq Jean-Luc, Hetru Charles, Lagueux Marie, Charlet Maurice, Hegy G, Dorsselaer Alan Van, Hoffmann Jules A
A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution Article de journal
Dans: J. Biol. Chem., vol. 268, no. 20, p. 14893–14897, 1993, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Carbohydrates, Cloning, DNA, Escherichia coli, Gas Chromatography-Mass Spectrometry, Glycopeptides, Glycosylation, hoffmann, M3i, Molecular
@article{bulet_novel_1993,
title = {A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution},
author = {Philippe Bulet and Jean-Luc Dimarcq and Charles Hetru and Marie Lagueux and Maurice Charlet and G Hegy and Alan Van Dorsselaer and Jules A Hoffmann},
issn = {0021-9258},
year = {1993},
date = {1993-07-01},
journal = {J. Biol. Chem.},
volume = {268},
number = {20},
pages = {14893--14897},
abstract = {One of the facets of the host defense of higher insects is the rapid and transient synthesis, following bacterial challenge or trauma, of a battery of potent antibacterial peptides (Steiner, H., Hultmark, D., Engström, A., Bennich, H., and Boman, H. G. (1981) Nature 292, 246-248). The best characterized of these peptides are the cecropins (ibid.), 4-kDa peptides devoid of cysteines, and the insect defensins (Hoffmann, J. A., and Hetru, C. (1992) Immunol. Today 13, 411-415), 4-kDa peptides with three intramolecular disulfide bridges. Several other inducible antibacterial peptides have been characterized only at the level of their amino acid sequences (Hoffmann, J. A., Dimarcq, J. L., and Bulet, P. (1992) Médecine & Sciences 8, 432-439). We report here the isolation of a novel 19-residue proline-rich inducible antibacterial peptide from Drosophila. In contrast to all previous reports on antibacterial peptides, this molecule carries a substitution as evidenced by molecular mass determinations; our data show that this reflects the O-glycosylation of a Thr residue by an N-acetylgalactosamine plus a galactose. A synthetic nonsubstituted peptide of identical amino acid sequence has an activity several times lower (5-10) than the native compound. Our data suggest that this substitution represents a post-translational modification essential for the full biological activity of this novel peptide.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Carbohydrates, Cloning, DNA, Escherichia coli, Gas Chromatography-Mass Spectrometry, Glycopeptides, Glycosylation, hoffmann, M3i, Molecular},
pubstate = {published},
tppubtype = {article}
}
One of the facets of the host defense of higher insects is the rapid and transient synthesis, following bacterial challenge or trauma, of a battery of potent antibacterial peptides (Steiner, H., Hultmark, D., Engström, A., Bennich, H., and Boman, H. G. (1981) Nature 292, 246-248). The best characterized of these peptides are the cecropins (ibid.), 4-kDa peptides devoid of cysteines, and the insect defensins (Hoffmann, J. A., and Hetru, C. (1992) Immunol. Today 13, 411-415), 4-kDa peptides with three intramolecular disulfide bridges. Several other inducible antibacterial peptides have been characterized only at the level of their amino acid sequences (Hoffmann, J. A., Dimarcq, J. L., and Bulet, P. (1992) Médecine & Sciences 8, 432-439). We report here the isolation of a novel 19-residue proline-rich inducible antibacterial peptide from Drosophila. In contrast to all previous reports on antibacterial peptides, this molecule carries a substitution as evidenced by molecular mass determinations; our data show that this reflects the O-glycosylation of a Thr residue by an N-acetylgalactosamine plus a galactose. A synthetic nonsubstituted peptide of identical amino acid sequence has an activity several times lower (5-10) than the native compound. Our data suggest that this substitution represents a post-translational modification essential for the full biological activity of this novel peptide.
1987
Debono M, Barnhart M, Carrell C B, Hoffmann Jules A, Occolowitz J L, Abbott B J, Fukuda D S, Hamill R L, Biemann K, Herlihy W C
A21978C, a complex of new acidic peptide antibiotics: isolation, chemistry, and mass spectral structure elucidation Article de journal
Dans: J. Antibiot., vol. 40, no. 6, p. 761–777, 1987, ISSN: 0021-8820.
Résumé | BibTeX | Étiquettes: Acylation, Amino Acids, Anti-Bacterial Agents, Chemical Phenomena, Chemistry, Chromatography, Cyclic, Fatty Acids, Gas Chromatography-Mass Spectrometry, High Pressure Liquid, hoffmann, Hydrolysis, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Conformation, Peptides, Spectrophotometry, Streptomyces
@article{debono_a21978c_1987,
title = {A21978C, a complex of new acidic peptide antibiotics: isolation, chemistry, and mass spectral structure elucidation},
author = {M Debono and M Barnhart and C B Carrell and Jules A Hoffmann and J L Occolowitz and B J Abbott and D S Fukuda and R L Hamill and K Biemann and W C Herlihy},
issn = {0021-8820},
year = {1987},
date = {1987-01-01},
journal = {J. Antibiot.},
volume = {40},
number = {6},
pages = {761--777},
abstract = {A21978C, produced by Streptomyces roseosporus, NRRL 11379, is a complex of new acidic lipopeptolide antibiotics which inhibits Gram-positive bacteria. HPLC separation of the various components from the purified complex resulted in the isolation of A21978C1, -C2 and -C3 (major components) and -C4, -C5, and -C0 (minor components). Each of these components was fermented with cultures of Actinoplanes utahensis (NRRL 12052) to give the identical inactive peptide ("A21978C nucleus") by removal of the fatty acid acyl groups from the N-terminus. This peptide was composed of 13 amino acids: L-kynurenine, L-threo-3-methylglutamic acid, L-asparagine, L-aspartic acid (3 residues), glycine (2 residues), L-tryptophan, L-ornithine, D-alanine, D-serine and L-threonine. The amino acid sequence was determined using a combination of the Edman degradation and gas chromatography mass spectrum (GC-MS) analysis of appropriately derivatized peptides obtained from partial hydrolysis. Each major component was shown to be acylated with a branched chain fatty acid at the N-terminus and the structure of this fatty acid was determined by 1H NMR and mass spectral methods. A structure for A21978C was assigned on the basis of this degradative and physico-chemical information.},
keywords = {Acylation, Amino Acids, Anti-Bacterial Agents, Chemical Phenomena, Chemistry, Chromatography, Cyclic, Fatty Acids, Gas Chromatography-Mass Spectrometry, High Pressure Liquid, hoffmann, Hydrolysis, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Conformation, Peptides, Spectrophotometry, Streptomyces},
pubstate = {published},
tppubtype = {article}
}
A21978C, produced by Streptomyces roseosporus, NRRL 11379, is a complex of new acidic lipopeptolide antibiotics which inhibits Gram-positive bacteria. HPLC separation of the various components from the purified complex resulted in the isolation of A21978C1, -C2 and -C3 (major components) and -C4, -C5, and -C0 (minor components). Each of these components was fermented with cultures of Actinoplanes utahensis (NRRL 12052) to give the identical inactive peptide ("A21978C nucleus") by removal of the fatty acid acyl groups from the N-terminus. This peptide was composed of 13 amino acids: L-kynurenine, L-threo-3-methylglutamic acid, L-asparagine, L-aspartic acid (3 residues), glycine (2 residues), L-tryptophan, L-ornithine, D-alanine, D-serine and L-threonine. The amino acid sequence was determined using a combination of the Edman degradation and gas chromatography mass spectrum (GC-MS) analysis of appropriately derivatized peptides obtained from partial hydrolysis. Each major component was shown to be acylated with a branched chain fatty acid at the N-terminus and the structure of this fatty acid was determined by 1H NMR and mass spectral methods. A structure for A21978C was assigned on the basis of this degradative and physico-chemical information.
1982
Hetru Charles, Kappler Christine, Hoffmann Jules A, Nearn R, Bang Lee, Horn D H
The biosynthetic pathway of ecdysone: studies with vitellogenic ovaries of Locusta migratoria (Orthoptera) Article de journal
Dans: Mol. Cell. Endocrinol., vol. 26, no. 1-2, p. 51–80, 1982, ISSN: 0303-7207.
Résumé | BibTeX | Étiquettes: Animals, Chromatography, Ecdysone, Female, Gas Chromatography-Mass Spectrometry, High Pressure Liquid, hoffmann, M3i, Orthoptera, Ovary
@article{hetru_biosynthetic_1982,
title = {The biosynthetic pathway of ecdysone: studies with vitellogenic ovaries of Locusta migratoria (Orthoptera)},
author = {Charles Hetru and Christine Kappler and Jules A Hoffmann and R Nearn and Lee Bang and D H Horn},
issn = {0303-7207},
year = {1982},
date = {1982-04-01},
journal = {Mol. Cell. Endocrinol.},
volume = {26},
number = {1-2},
pages = {51--80},
abstract = {Ovaries of adult females of Locusta migratoria synthesize impressive amounts of the steroid hormone ecdysone (and related ecdysteroids) during the late phases of vitellogenesis. The present study, aimed at elucidating the sequence of the biosynthetic steps that lead from cholesterol to ecdysone, has taken benefit of this remarkable biological model by using a double approach: (1) isolation and physico-chemical identification of endogenous biogenetic intermediates; (2) metabolic study of labelled putative precursor molecules. The data presented in this paper lead us to propose the following sequence of events: conversion of cholesterol to 3 beta-hydroxy-5 beta-cholest-7-en-6-one (via several intermediates not identified in this study) followed by 14 beta-hydroxylation to 3 beta, 14 alpha-dihydroxy-5 beta-cholest-7-en-6-one; hydroxylation on the side-chain at C-25 and C-22 (in this order) to 2-deoxyecdysone; hydroxylation at C-2 to ecdysone.},
keywords = {Animals, Chromatography, Ecdysone, Female, Gas Chromatography-Mass Spectrometry, High Pressure Liquid, hoffmann, M3i, Orthoptera, Ovary},
pubstate = {published},
tppubtype = {article}
}
Ovaries of adult females of Locusta migratoria synthesize impressive amounts of the steroid hormone ecdysone (and related ecdysteroids) during the late phases of vitellogenesis. The present study, aimed at elucidating the sequence of the biosynthetic steps that lead from cholesterol to ecdysone, has taken benefit of this remarkable biological model by using a double approach: (1) isolation and physico-chemical identification of endogenous biogenetic intermediates; (2) metabolic study of labelled putative precursor molecules. The data presented in this paper lead us to propose the following sequence of events: conversion of cholesterol to 3 beta-hydroxy-5 beta-cholest-7-en-6-one (via several intermediates not identified in this study) followed by 14 beta-hydroxylation to 3 beta, 14 alpha-dihydroxy-5 beta-cholest-7-en-6-one; hydroxylation on the side-chain at C-25 and C-22 (in this order) to 2-deoxyecdysone; hydroxylation at C-2 to ecdysone.
