Publications
1996
Fehlbaum P, Bulet Philippe, Chernysh S, Briand J P, Roussel J P, Letellier L, Hetru Charles, Hoffmann Jules A
Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides Article de journal
Dans: Proc. Natl. Acad. Sci. U.S.A., vol. 93, no. 3, p. 1221–1225, 1996, ISSN: 0027-8424.
Résumé | BibTeX | Étiquettes: Amino Acid, Amphibian Proteins, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Cyclic, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, hoffmann, M3i, Mass Spectrometry, Microbial Sensitivity Tests, Peptides, Ranidae, Sequence Homology, Skin, Structure-Activity Relationship
@article{fehlbaum_structure-activity_1996,
title = {Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides},
author = {P Fehlbaum and Philippe Bulet and S Chernysh and J P Briand and J P Roussel and L Letellier and Charles Hetru and Jules A Hoffmann},
issn = {0027-8424},
year = {1996},
date = {1996-02-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {93},
number = {3},
pages = {1221--1225},
abstract = {Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family. The insect and frog peptides have in common a C-terminally located disulfide bridge delineating a cationic loop. The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense peptide. An all-D-enantiomer is nearly inactive against Gram-negative bacteria and some Gram-positive strains but is fully active against fungi and other Gram-positive bacteria, suggesting that more than one mechanism accounts for the antimicrobial activity of this peptide. Studies with truncated synthetic isoforms underline the role of the C-terminal loop and flanking residues for the activity of this molecule for which we propose the name thanatin.},
keywords = {Amino Acid, Amphibian Proteins, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Cyclic, Fungi, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemiptera, hoffmann, M3i, Mass Spectrometry, Microbial Sensitivity Tests, Peptides, Ranidae, Sequence Homology, Skin, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}
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}
}