Publications
1990
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 Journal Article
In: EMBO J., vol. 9, no. 8, pp. 2507–2515, 1990, ISSN: 0261-4189.
Abstract | BibTeX | Tags: 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}
}
Lagueux Marie, Lwoff L, Meister Marie, Goltzené F, Hoffmann Jules A
cDNAs from neurosecretory cells of brains of Locusta migratoria (Insecta, Orthoptera) encoding a novel member of the superfamily of insulins Journal Article
In: Eur. J. Biochem., vol. 187, no. 1, pp. 249–254, 1990, ISSN: 0014-2956.
Abstract | BibTeX | Tags: Animals, Base Sequence, DNA, Genes, Grasshoppers, hoffmann, Humans, Insulin, M3i, Multigene Family, Nervous System, Neuropeptides, Neurosecretory Systems, Nucleic Acid, Nucleic Acid Hybridization, Oligonucleotide Probes, RNA, Sequence Homology
@article{lagueux_cdnas_1990,
title = {cDNAs from neurosecretory cells of brains of Locusta migratoria (Insecta, Orthoptera) encoding a novel member of the superfamily of insulins},
author = {Marie Lagueux and L Lwoff and Marie Meister and F Goltzené and Jules A Hoffmann},
issn = {0014-2956},
year = {1990},
date = {1990-01-01},
journal = {Eur. J. Biochem.},
volume = {187},
number = {1},
pages = {249--254},
abstract = {From neurohaemal lobes of corpora cardiaca of Locusta migratoria a 5-kDa peptide has been isolated and its sequence established [see the accompanying paper, by Hietter et al. (1990) Eur. J. Biochem. 187, 241-247]. We have designed oligonucleotide probes from the peptide sequence of this molecule and screened a library prepared from mRNA of the neurosecretory cell region of the brain of this insect. Several positive cDNAs were isolated, the combined nucleotide sequences of which predict a large precursor of 145 residues (15770 Da) containing the newly isolated 5-kDa peptide. The peptide is flanked by regions homologous to the A and B chains of the superfamily of insulins. The overall organization of the precursor is as follows: signal peptide/domain homologous to the B chain of insulins/C (connecting)-peptide (corresponding to the newly isolated 5-kDa peptide)/domain homologous to the A chain of insulins. The numbers and relative positions of the cysteines of the Locusta peptide are equivalent to those of the other members of the insulin superfamily and most of the hydrophobic core residues are conserved.},
keywords = {Animals, Base Sequence, DNA, Genes, Grasshoppers, hoffmann, Humans, Insulin, M3i, Multigene Family, Nervous System, Neuropeptides, Neurosecretory Systems, Nucleic Acid, Nucleic Acid Hybridization, Oligonucleotide Probes, RNA, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}