Dimarcq Jean-Luc, Zachary Daniel, Hoffmann Jules A, Hoffmann Danièle, Reichhart Jean-Marc
Insect immunity: expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae Article de journal
Dans: EMBO J., vol. 9, no. 8, p. 2507–2515, 1990, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Blood Proteins, Cloning, Defensins, Diptera, Gene Expression, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Molecular, Nucleic Acid Hybridization, Oligonucleotide Probes, Protein Conformation, reichhart
@article{dimarcq_insect_1990,
title = {Insect immunity: expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae},
author = {Jean-Luc Dimarcq and Daniel Zachary and Jules A Hoffmann and Danièle Hoffmann and Jean-Marc Reichhart},
issn = {0261-4189},
year = {1990},
date = {1990-08-01},
journal = {EMBO J.},
volume = {9},
number = {8},
pages = {2507--2515},
abstract = {Injections of low doses of bacteria into larvae of Phormia terranovae induce the appearance of potent bactericidal peptides in the blood, among which predominate the anti-Gram positive insect defensins and the anti-Gram negative diptericins. Insect defensins show significant homologies to mammalian (including human) microbicidal peptides present in polymorphonuclear leukocytes and macrophages. We report the molecular cloning of cDNAs and primer extension studies which indicate that insect defensin is produced as a prepro-peptide yielding mature defensin A (40 residues) after cleavage of a putative signal peptide (23 residues) and a prosequence (34 residues). Previous studies have established that diptericin (82 residues) is matured from a pre-peptide by cleavage of a putative signal peptide (19 residues) and C-terminal amidation. Using oligonucleotide probes complementary to the sequences of the mRNAs for defensin and diptericin, we show by in situ hybridization that both antibacterial peptides are concomitantly synthesized by the same cells: thrombocytoids, a specialized blood cell type, and adipocytes. Transcriptional studies based on hybridization of RNAs to cDNAs of defensin and diptericin indicate that the transcription of both genes is induced regardless of the nature of the stimulus (injection of Gram positive or Gram negative bacteria, lipopolysaccharides). Even a sterile injury applied to axenically raised larvae is efficient in inducing the transcription of both genes suggesting that the local disruption of the integument aspecifically initiates a signalling mechanism which the thrombocytoids and the adipocytes are able to interpret. The transcription of immune genes is relatively short lived and a second challenge yields a response similar to that of the first stimulus, indicating that the experimental insects do not keep a 'memory' of their first injection.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Blood Proteins, Cloning, Defensins, Diptera, Gene Expression, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Molecular, Nucleic Acid Hybridization, Oligonucleotide Probes, Protein Conformation, reichhart},
pubstate = {published},
tppubtype = {article}
}
Wicker C, Reichhart Jean-Marc, Hoffmann Danièle, Hultmark D, Samakovlis C, Hoffmann Jules A
Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides Article de journal
Dans: J. Biol. Chem., vol. 265, no. 36, p. 22493–22498, 1990, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Diptera, DNA, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, M3i, Molecular, Multigene Family, Nucleic Acid, Oligonucleotide Probes, reichhart, Sequence Homology
@article{wicker_insect_1990,
title = {Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides},
author = {C Wicker and Jean-Marc Reichhart and Danièle Hoffmann and D Hultmark and C Samakovlis and Jules A Hoffmann},
issn = {0021-9258},
year = {1990},
date = {1990-01-01},
journal = {J. Biol. Chem.},
volume = {265},
number = {36},
pages = {22493--22498},
abstract = {Drosophila shows an immune response when challenged by injection of low doses of bacteria. To date, the molecules involved in this immune reaction have remained elusive, with the exception of cecropins (4-kDa antibacterial peptides initially isolated from the moth Hyalophora cecropia) for which three closely related genes have been characterized recently. We report the molecular cloning and sequencing of a cDNA from a library of immune Drosophila which encodes a novel member of the family of diptericins (9-kDa antibacterial peptides initially isolated from the fly Phormia terranovae). Transcripts for the Drosophila diptericin are detected 2 h after injection of bacteria. They are apparently derived from a single gene mapping at position 56 A on the right arm of the second chromosome. We discuss the existence of a distant relationship between the diptericins and two other groups of anti-bacterial insect proteins, the attacins, and the sarcotoxins II.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Diptera, DNA, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, M3i, Molecular, Multigene Family, Nucleic Acid, Oligonucleotide Probes, reichhart, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Reichhart Jean-Marc, Essrich M, Dimarcq Jean-Luc, Hoffmann Danièle, Hoffmann Jules A, Lagueux Marie
Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera). Transcriptional profiles during immunization Article de journal
Dans: Eur. J. Biochem., vol. 182, no. 2, p. 423–427, 1989, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Bacterial Proteins, Base Sequence, Blotting, Diptera, DNA, Endoribonucleases, Enterobacter, Enterobacteriaceae, Gene Expression Regulation, Genes, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, messenger, MHC Class II, Northern, reichhart, Ribonuclease H, RNA, Transcription
@article{reichhart_insect_1989,
title = {Insect immunity. Isolation of cDNA clones corresponding to diptericin, an inducible antibacterial peptide from Phormia terranovae (Diptera). Transcriptional profiles during immunization},
author = {Jean-Marc Reichhart and M Essrich and Jean-Luc Dimarcq and Danièle Hoffmann and Jules A Hoffmann and Marie Lagueux},
issn = {0014-2956},
year = {1989},
date = {1989-01-01},
journal = {Eur. J. Biochem.},
volume = {182},
number = {2},
pages = {423--427},
abstract = {We have previously isolated and characterized a family of novel 8-kDa cationic antibacterial peptides synthesized by larvae of Phormia terranovae (Diptera) in response to various injuries. These molecules have been named diptericins. The peptide sequence of diptericin A was used to prepare oligonucleotides for screening cDNA libraries and we report in the present paper the isolation of several cDNA clones encoding diptericin. The analysis of the nucleotide sequences indicates that diptericin is synthesized as a prepeptide which is matured in two steps: (a) cleavage of a signal peptide and (b) amidation of the C-terminal residue. Interestingly, the 3' untranslated region of the mRNA contains a consensus sequence TTATTTAT which is also observed in the mRNA of another insect antibacterial peptide (attacin-related sarcotoxin IIA) and in mRNAs encoding proteins related to the inflammatory response in mammals. Our data illustrate that diptericins form a polymorphic family of immune peptides. The transcription of the diptericin genes is rapidly induced in the fat body after inoculation of bacteria, as evidenced by the transcriptional profile.},
keywords = {Animals, Anti-Bacterial Agents, Bacterial Proteins, Base Sequence, Blotting, Diptera, DNA, Endoribonucleases, Enterobacter, Enterobacteriaceae, Gene Expression Regulation, Genes, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, messenger, MHC Class II, Northern, reichhart, Ribonuclease H, RNA, Transcription},
pubstate = {published},
tppubtype = {article}
}
Dimarcq Jean-Luc, Keppi E, Dunbar B, Lambert J, Reichhart Jean-Marc, Hoffmann Danièle, Rankine S M, Fothergill J E, Hoffmann Jules A
Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A Article de journal
Dans: Eur. J. Biochem., vol. 171, no. 1-2, p. 17–22, 1988, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Amino Acids, Animals, Anti-Bacterial Agents, Diptera, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, Isoelectric Point, Larva, M3i, reichhart
@article{dimarcq_insect_1988,
title = {Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A},
author = {Jean-Luc Dimarcq and E Keppi and B Dunbar and J Lambert and Jean-Marc Reichhart and Danièle Hoffmann and S M Rankine and J E Fothergill and Jules A Hoffmann},
issn = {0014-2956},
year = {1988},
date = {1988-01-01},
journal = {Eur. J. Biochem.},
volume = {171},
number = {1-2},
pages = {17--22},
abstract = {Injury or injection of live bacteria into third instar larvae of the dipteran insect Phormia terranovae results in the appearance in the haemolymph of at least five groups of heat-stable, more or less basic peptides with antibacterial activity against Escherichia coli. Three of these peptides have been purified. The amino acid sequence has been completely established for one of these and partially (first 40 residues from the N-terminus) for the two others. The sequences show marked homologies indicating that the three peptides belong to a common family. They are not related to other known antibacterial peptides from insects [lysozymes, cecropins (including sarcotoxin I) and attacins]. We propose the name of diptericins for this new family of antibiotic molecules.},
keywords = {Amino Acids, Animals, Anti-Bacterial Agents, Diptera, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, Isoelectric Point, Larva, M3i, reichhart},
pubstate = {published},
tppubtype = {article}
}