Gross I, Georgel Philippe, Kappler Christine, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin Article de journal
Dans: Nucleic Acids Res., vol. 24, no. 7, p. 1238–1245, 1996, ISSN: 0305-1048.
Résumé | BibTeX | Étiquettes: Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation
@article{gross_drosophila_1996,
title = {Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin},
author = {I Gross and Philippe Georgel and Christine Kappler and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0305-1048},
year = {1996},
date = {1996-04-01},
journal = {Nucleic Acids Res.},
volume = {24},
number = {7},
pages = {1238--1245},
abstract = {In Drosophila, bacterial challenge induces the rapid transcription of several genes encoding potent antibacterial peptides. The upstream sequences of the diptericin and cecropin Al genes, which have been investigated in detail, contain two, respectively one sequence element homologous to the binding site of the mammalian nuclear factor kappaB. These elements have been shown to be mandatory for immune-induced transcription of both genes. Functional studies have shown that these kappaB-related elements can be the target for the Drosophila Rel proteins dorsal and Dif. Here we present a comparative analysis of the transactivating capacities of these proteins on reporter genes fused to either the diptericin or the cecropin kappaB-related motifs. We conclude from our results: (i) the kappaB motifs of the diptericin and cecropin genes are not functionally equivalent; (ii) the dorsal and Dif proteins have distinct DNA-binding characteristics; (iii) dorsal and Dif can heterodimerize in vitro; (iv) mutants containing no copies of dorsal and a single copy of Dif retain their full capacity to express the diptericin and cecropin genes in response to challenge.},
keywords = {Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}
Lemaitre Bruno, Nicolas E, Michaut Lydia, Reichhart Jean-Marc, Hoffmann Jules A
The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults Article de journal
Dans: Cell, vol. 86, no. 6, p. 973–983, 1996, ISSN: 0092-8674.
Résumé | BibTeX | Étiquettes: Animals, Antifungal Agents, Cell Surface, DNA-Binding Proteins, Fungi, Gene Expression, Genes, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Membrane Glycoproteins, MHC Class II, Mutation, Mycoses, NF-kappa B, Phosphoproteins, Proteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors
@article{lemaitre_dorsoventral_1996,
title = {The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults},
author = {Bruno Lemaitre and E Nicolas and Lydia Michaut and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0092-8674},
year = {1996},
date = {1996-01-01},
journal = {Cell},
volume = {86},
number = {6},
pages = {973--983},
abstract = {The cytokine-induced activation cascade of NF-kappaB in mammals and the activation of the morphogen dorsal in Drosophila embryos show striking structural and functional similarities (Toll/IL-1, Cactus/I-kappaB, and dorsal/NF-kappaB). Here we demonstrate that these parallels extend to the immune response of Drosophila. In particular, the intracellular components of the dorsoventral signaling pathway (except for dorsal) and the extracellular Toll ligand, spätzle, control expression of the antifungal peptide gene drosomycin in adults. We also show that mutations in the Toll signaling pathway dramatically reduce survival after fungal infection. Antibacterial genes are induced either by a distinct pathway involving the immune deficiency gene (imd) or by combined activation of both imd and dorsoventral pathways.},
keywords = {Animals, Antifungal Agents, Cell Surface, DNA-Binding Proteins, Fungi, Gene Expression, Genes, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Membrane Glycoproteins, MHC Class II, Mutation, Mycoses, NF-kappa B, Phosphoproteins, Proteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Lemaitre Bruno, Kromer-Metzger E, Michaut Lydia, Nicolas E, Meister Marie, Georgel Philippe, Reichhart Jean-Marc, Hoffmann Jules A
A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense Article de journal
Dans: Proc. Natl. Acad. Sci. U.S.A., vol. 92, no. 21, p. 9465–9469, 1995, ISSN: 0027-8424.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacterial Infections, Base Sequence, Gene Expression Regulation, Genes, Glycopeptides, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Male, Mutation, Mycoses, Nucleic Acid, Peptides, Protein Binding, Recessive, Regulatory Sequences, reichhart, Reporter, Survival Analysis
@article{lemaitre_recessive_1995,
title = {A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense},
author = {Bruno Lemaitre and E Kromer-Metzger and Lydia Michaut and E Nicolas and Marie Meister and Philippe Georgel and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0027-8424},
year = {1995},
date = {1995-10-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {92},
number = {21},
pages = {9465--9469},
abstract = {In this paper we report a recessive mutation, immune deficiency (imd), that impairs the inducibility of all genes encoding antibacterial peptides during the immune response of Drosophila. When challenged with bacteria, flies carrying this mutation show a lower survival rate than wild-type flies. We also report that, in contrast to the antibacterial peptides, the antifungal peptide drosomycin remains inducible in a homozygous imd mutant background. These results point to the existence of two different pathways leading to the expression of two types of target genes, encoding either the antibacterial peptides or the antifungal peptide drosomycin.},
keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacterial Infections, Base Sequence, Gene Expression Regulation, Genes, Glycopeptides, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Male, Mutation, Mycoses, Nucleic Acid, Peptides, Protein Binding, Recessive, Regulatory Sequences, reichhart, Reporter, Survival Analysis},
pubstate = {published},
tppubtype = {article}
}
Bulet Philippe, Hegy G, Lambert J, van Dorsselaer Alan, Hoffmann Jules A, Hetru Charles
Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity Article de journal
Dans: Biochemistry, vol. 34, no. 22, p. 7394–7400, 1995, ISSN: 0006-2960.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Carbohydrate Sequence, Carbohydrates, Diptera, Escherichia coli, Glycopeptides, Hemolymph, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mass Spectrometry, Plants, Trisaccharides
@article{bulet_insect_1995,
title = {Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity},
author = {Philippe Bulet and G Hegy and J Lambert and Alan van Dorsselaer and Jules A Hoffmann and Charles Hetru},
issn = {0006-2960},
year = {1995},
date = {1995-06-01},
journal = {Biochemistry},
volume = {34},
number = {22},
pages = {7394--7400},
abstract = {A bacterial challenge of larvae of the dipteran insect Phormia terranovae induces the rapid synthesis of diptericin, an antibacterial polypeptide, previously characterized at the amino acid level and indirectly by cDNA cloning studies. This 82-residue polypeptide consists of an N-terminal proline-rich domain and a central and C-terminal glycine-rich domain. Using liquid chromatography coupled to electrospray ionization-mass spectrometry, we demonstrate here that this molecule is more complex than anticipated and carries two O-substitutions on threonine residues, one in the proline-rich domain (residue 10) and one in the glycine-rich domain (residue 54). These substitutions consist of identical trisaccharides: glucose--textgreatergalactose--textgreaterN-acetylgalactosamine--textgreater(threonine). Treatment of diptericin with O-glycosidase, which selectively removes the substitutions without altering the polypeptide proper, abolishes the antibacterial activity, indicating that this posttranslational modification is essential for biological activity of the polypeptide. We also show that diptericin is posttranslationally modified by a C-terminal amidation.},
keywords = {Animals, Anti-Bacterial Agents, Carbohydrate Sequence, Carbohydrates, Diptera, Escherichia coli, Glycopeptides, Hemolymph, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mass Spectrometry, Plants, Trisaccharides},
pubstate = {published},
tppubtype = {article}
}
Cornet B, Bonmatin J M, Hetru Charles, Hoffmann Jules A, Ptak M, Vovelle F
Refined three-dimensional solution structure of insect defensin A Article de journal
Dans: Structure, vol. 3, no. 5, p. 435–448, 1995, ISSN: 0969-2126.
Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Bacteriolysis, Chemistry, Defensins, Diptera, Gram-Positive Bacteria, hoffmann, Hydrogen Bonding, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Physical, Physicochemical Phenomena, Protein Conformation, Recombinant Proteins, Sequence Homology, Solutions, Structure-Activity Relationship
@article{cornet_refined_1995,
title = {Refined three-dimensional solution structure of insect defensin A},
author = {B Cornet and J M Bonmatin and Charles Hetru and Jules A Hoffmann and M Ptak and F Vovelle},
issn = {0969-2126},
year = {1995},
date = {1995-05-01},
journal = {Structure},
volume = {3},
number = {5},
pages = {435--448},
abstract = {BACKGROUND: Insect defensin A is a basic 4 kDa protein secreted by Phormia terranovae larvae in response to bacterial challenges or injuries. Previous biological tests suggest that the bacterial cytoplasmic membrane is the target of defensin A. The structural study of this protein is the first step towards establishing a structure-activity relationship and forms the basis for understanding its antibiotic activity at the molecular level. RESULTS: We describe a refined model of the three-dimensional structure of defensin A derived from an extensive analysis of 786 inter-proton nuclear Overhauser effects. The backbone fold involves an N-terminal loop and an alpha-helical fragment followed by an antiparallel beta-structure. The helix and the beta-structure are connected by two of the three disulphide bridges present in defensin A, forming a so-called 'cysteine-stabilized alpha beta' (CS alpha beta) motif. The N-terminal loop, which is locally well defined, can occupy different positions with respect to the other moieties of the molecule. CONCLUSIONS: The CS alpha beta motif, which forms the core of the defensin A structure, appears to be a common organization for several families of small proteins with toxic properties. The distribution of amino acid side chains in the protein structure creates several hydrophobic or hydrophilic patches. This leads us to propose that the initial step in the action of positively charged defensin A molecules with cytoplasmic membranes may involve interactions with acidic phospholipids.},
keywords = {Amino Acid, Animals, Bacteriolysis, Chemistry, Defensins, Diptera, Gram-Positive Bacteria, hoffmann, Hydrogen Bonding, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Physical, Physicochemical Phenomena, Protein Conformation, Recombinant Proteins, Sequence Homology, Solutions, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}
Georgel Philippe, Kappler Christine, Langley E, Gross I, Nicolas E, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter Article de journal
Dans: Nucleic Acids Res., vol. 23, no. 7, p. 1140–1145, 1995, ISSN: 0305-1048.
Résumé | BibTeX | Étiquettes: Animals, Base Sequence, CCAAT-Enhancer-Binding Proteins, DNA, DNA-Binding Proteins, Genes, Genetic, hoffmann, Immunity, Insect, Insect Hormones, Insect Proteins, interferons, Lipopolysaccharides, M3i, NF-kappa B, Nuclear Proteins, Plasmids, Promoter Regions, reichhart, Up-Regulation
@article{georgel_drosophila_1995,
title = {Drosophila immunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter},
author = {Philippe Georgel and Christine Kappler and E Langley and I Gross and E Nicolas and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0305-1048},
year = {1995},
date = {1995-04-01},
journal = {Nucleic Acids Res.},
volume = {23},
number = {7},
pages = {1140--1145},
abstract = {Bacterial challenge of larvae or adults of Drosophila induces the rapid transcription of several genes encoding antibacterial peptides with a large spectrum of activity. One of these peptides, the 82-residue anti-gram negative diptericin, is encoded by a single intronless gene and we are investigating the control of expression of this gene. Previous studies using both transgenic experiments and footprint analysis have highlighted the role in the induction of this gene of a 30 nucleotide region which contains three partially overlapping motifs with sequence homology to mammalian NF-kappa B and NF-IL6 response elements and to the GAAANN sequence present in the interferon consensus response elements of some mammalian interferon-induced genes. We now show that the latter sequence binds in immune responsive tissues (fat body, blood cells) of Drosophila a approximately 45 kDa polypeptide which cross-reacts with a polyserum directed against mammalian interferon Regulatory Factor-I. Using a transfection assay of Drosophila tumorous blood cells, we show that the GAAANN sequence positively regulates the activity of the diptericin promoter. We propose that this motif cooperatively interacts with the other response elements in the regulation of the diptericin gene expression.},
keywords = {Animals, Base Sequence, CCAAT-Enhancer-Binding Proteins, DNA, DNA-Binding Proteins, Genes, Genetic, hoffmann, Immunity, Insect, Insect Hormones, Insect Proteins, interferons, Lipopolysaccharides, M3i, NF-kappa B, Nuclear Proteins, Plasmids, Promoter Regions, reichhart, Up-Regulation},
pubstate = {published},
tppubtype = {article}
}
Lemaitre Bruno, Meister Marie, Govind S, Georgel Philippe, Steward R, Reichhart Jean-Marc, Hoffmann Jules A
Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila Article de journal
Dans: EMBO J., vol. 14, no. 3, p. 536–545, 1995, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Biological Transport, Cell Nucleus, Cell Surface, DNA-Binding Proteins, Fat Body, Gene Expression Regulation, Genetic, hoffmann, Immunity, Immunohistochemistry, Insect Hormones, Insect Proteins, M3i, Melanins, Membrane Glycoproteins, Mutation, Neoplasms, Nuclear Proteins, Phosphoproteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors, Transcription, Transcription Factors
@article{lemaitre_functional_1995,
title = {Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila},
author = {Bruno Lemaitre and Marie Meister and S Govind and Philippe Georgel and R Steward and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0261-4189},
year = {1995},
date = {1995-01-01},
journal = {EMBO J.},
volume = {14},
number = {3},
pages = {536--545},
abstract = {In addition to its function in embryonic development, the NF-kappa B/rel-related gene dorsal (dl) of Drosophila is expressed in larval and adult fat body where its RNA expression is enhanced upon injury. Injury also leads to a rapid nuclear translocation of dl from the cytoplasm in fat body cells. Here we present data which strongly suggest that the nuclear localization of dl during the immune response is controlled by the Toll signaling pathway, comprising gene products that participate in the intracellular part of the embryonic dorsoventral pathway. We also report that in mutants such as Toll or cactus, which exhibit melanotic tumor phenotypes, dl is constitutively nuclear. Together, these results point to a potential link between the Toll signaling pathway and melanotic tumor induction. Although dl has been shown previously to bind to kappa B-related motifs within the promoter of the antibacterial peptide coding gene diptericin, we find that injury-induced expression of diptericin can occur in the absence of dl. Furthermore, the melanotic tumor phenotype of Toll and cactus is not dl dependent. These data underline the complexity of the Drosophila immune response. Finally, we observed that like other rel proteins, dl can control the level of its own transcription.},
keywords = {Animals, Anti-Bacterial Agents, Anti-Infective Agents, Antimicrobial Cationic Peptides, Biological Transport, Cell Nucleus, Cell Surface, DNA-Binding Proteins, Fat Body, Gene Expression Regulation, Genetic, hoffmann, Immunity, Immunohistochemistry, Insect Hormones, Insect Proteins, M3i, Melanins, Membrane Glycoproteins, Mutation, Neoplasms, Nuclear Proteins, Phosphoproteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Ferrandon Dominique, Elphick L, Nüsslein-Volhard C, Johnston St D
Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner Article de journal
Dans: Cell, vol. 79, no. 7, p. 1221–1232, 1994, ISSN: 0092-8674.
Résumé | BibTeX | Étiquettes: Animals, Base Sequence, Cell Polarity, ferrandon, Homeodomain Proteins, Insect Hormones, M3i, messenger, Microtubules, Nucleic Acid Conformation, Oocytes, RNA, RNA-Binding Proteins, Trans-Activators
@article{ferrandon_staufen_1994b,
title = {Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner},
author = {Dominique Ferrandon and L Elphick and C Nüsslein-Volhard and St D Johnston},
issn = {0092-8674},
year = {1994},
date = {1994-12-01},
journal = {Cell},
volume = {79},
number = {7},
pages = {1221--1232},
abstract = {Staufen protein is required in order to anchor bicoid (bcd) mRNA at the anterior pole of the Drosophila egg. Here we show that staufen protein colocalizes with bcd mRNA at the anterior, and that this localization depends upon its association with the mRNA. Upon injection into the embryo, bcd transcripts specifically interact with staufen, and we have mapped the sequences required to three regions of the 3'UTR, each of which is predicted to form a long stem-loop. The resulting staufen-bcd 3'UTR complexes form particles that show a microtubule-dependent localization. Since staufen is also transported with oskar (osk) mRNA during oogenesis, staufen associates specifically with both osk and bcd mRNAs to mediate their localizations, but at two distinct stages of development.},
keywords = {Animals, Base Sequence, Cell Polarity, ferrandon, Homeodomain Proteins, Insect Hormones, M3i, messenger, Microtubules, Nucleic Acid Conformation, Oocytes, RNA, RNA-Binding Proteins, Trans-Activators},
pubstate = {published},
tppubtype = {article}
}
Meister Marie, Braun A, Kappler Christine, Reichhart Jean-Marc, Hoffmann Jules A
Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter Article de journal
Dans: EMBO J., vol. 13, no. 24, p. 5958–5966, 1994, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Base Sequence, beta-Galactosidase, DNA Mutational Analysis, Female, Gene Expression Regulation, Genetic, Genetically Modified, Germ Cells, hoffmann, Insect Hormones, Insect Proteins, M3i, Male, Models, Nucleic Acid, Promoter Regions, Recombinant Fusion Proteins, reichhart, Repetitive Sequences, Transformation
@article{meister_insect_1994,
title = {Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter},
author = {Marie Meister and A Braun and Christine Kappler and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0261-4189},
year = {1994},
date = {1994-12-01},
journal = {EMBO J.},
volume = {13},
number = {24},
pages = {5958--5966},
abstract = {Diptericins are antibacterial polypeptides which are strongly induced in the fat body and blood cells of dipteran insects in response to septic injury. The promoter of the single-copy, intronless diptericin gene of Drosophila contains several nucleotide sequences homologous to mammalian cis-regulatory motifs involved in the control of acute phase response genes. Extending our previous studies on the expression of the diptericin gene, we now report a quantitative analysis of the contribution of various putative regulatory elements to the bacterial inducibility of this gene, based on the generation of 60 transgenic fly lines carrying different elements fused to a reporter gene. Our data definitively identify two Kappa B-related motifs in the proximal promoter as the sites conferring inducibility and tissue-specific expression to the diptericin gene. These motifs alone, however, mediate only minimal levels of expression. Additional proximal regulatory elements are necessary to attain some 20% of the full response and we suspect a role for sequences homologous to mammalian IL6 response elements and interferon-gamma responsive sites in this up-regulation. The transgenic experiments also reveal the existence of a distal regulatory element located upstream of -0.6 kb which increases the level of expression by a factor of five.},
keywords = {Animals, Anti-Infective Agents, Base Sequence, beta-Galactosidase, DNA Mutational Analysis, Female, Gene Expression Regulation, Genetic, Genetically Modified, Germ Cells, hoffmann, Insect Hormones, Insect Proteins, M3i, Male, Models, Nucleic Acid, Promoter Regions, Recombinant Fusion Proteins, reichhart, Repetitive Sequences, Transformation},
pubstate = {published},
tppubtype = {article}
}
Georgel Philippe, Meister Marie, Kappler Christine, Lemaitre Bruno, Reichhart Jean-Marc, Hoffmann Jules A
Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements Article de journal
Dans: Biochem. Biophys. Res. Commun., vol. 197, no. 2, p. 508–517, 1993, ISSN: 0006-291X.
Résumé | Liens | BibTeX | Étiquettes: Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart
@article{georgel_insect_1993,
title = {Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements},
author = {Philippe Georgel and Marie Meister and Christine Kappler and Bruno Lemaitre and Jean-Marc Reichhart and Jules A Hoffmann},
doi = {10.1006/bbrc.1993.2508},
issn = {0006-291X},
year = {1993},
date = {1993-12-01},
journal = {Biochem. Biophys. Res. Commun.},
volume = {197},
number = {2},
pages = {508--517},
abstract = {We are using the diptericin gene as a model system to study the control of expression of the genes encoding antibacterial peptides during the Drosophila immune reaction. In order to investigate the putative regulatory regions in the diptericin promoter, we performed DNaseI footprinting experiments combined with gel-shift assays in two inducible systems: the larval fat body and a tumorous Drosophila blood cell line. Our results confirm the importance of kappa B-like elements previously described in the immune response of insects and reveal for the first time the involvement of other regions containing sequences homologous to mammalian acute-phase response elements.},
keywords = {Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart},
pubstate = {published},
tppubtype = {article}
}
Hoffmann Jules A, Hetru Charles, Reichhart Jean-Marc
The humoral antibacterial response of Drosophila Article de journal
Dans: FEBS Lett., vol. 325, no. 1-2, p. 63–66, 1993, ISSN: 0014-5793.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Genes, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, reichhart, Sequence Homology
@article{hoffmann_humoral_1993,
title = {The humoral antibacterial response of Drosophila},
author = {Jules A Hoffmann and Charles Hetru and Jean-Marc Reichhart},
issn = {0014-5793},
year = {1993},
date = {1993-06-01},
journal = {FEBS Lett.},
volume = {325},
number = {1-2},
pages = {63--66},
abstract = {Drosophila, like other insects, responds to the injection of bacteria by the rapid and transient synthesis of a battery of potent antibacterial peptides. Only a few of these peptides have been fully characterized to date. We review our recent data on the control of the expression of a gene encoding one of the induced peptides, i.e. diptericin. Our data highlight the role of proximal cis-regulatory motifs similar to regulatory elements binding NF-kappa B and NF-IL6 in promoters of some immune genes of mammals. We argue that the Drosophila host defense is homologous to the mammalian acute phase response.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Genes, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, reichhart, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
Kappler Christine, Meister Marie, Lagueux Marie, Gateff E, Hoffmann Jules A, Reichhart Jean-Marc
Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila Article de journal
Dans: EMBO J., vol. 12, no. 4, p. 1561–1568, 1993, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection
@article{kappler_insect_1993,
title = {Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila},
author = {Christine Kappler and Marie Meister and Marie Lagueux and E Gateff and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {0261-4189},
year = {1993},
date = {1993-04-01},
journal = {EMBO J.},
volume = {12},
number = {4},
pages = {1561--1568},
abstract = {The Drosophila diptericin gene codes for a 9 kDa antibacterial peptide and is rapidly and transiently expressed in larvae and adults after bacterial challenge. It is also induced in a tumorous Drosophila blood cell line by the addition of lipopolysaccharide (LPS). The promoter of this gene contains two 17 bp repeats located closely upstream of the TATA-box and harbouring a decameric kappa B-related sequence. This study reports that the replacement of the two 17 bp repeats by random sequences abolishes bacteria inducibility in transgenic fly lines. In transfected tumorous blood cells, the replacement of both or either of the 17 bp motifs reduces dramatically LPS inducibility, whereas multiple copies significantly increase the level of transcriptional activation by LPS challenge. A specific DNA-protein binding activity is evidenced in cytoplasmic and nuclear extracts of induced blood cells and fat body. It is absent in controls. It is proposed that induction of the diptericin gene mediated by the two 17 bp repeats occurs via a mechanism similar to that of mammalian NF-kappa B.},
keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection},
pubstate = {published},
tppubtype = {article}
}
Reichhart Jean-Marc, Meister Marie, Dimarcq Jean-Luc, Zachary Daniel, Hoffmann Danièle, Ruiz C, Richards G, Hoffmann Jules A
Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter Article de journal
Dans: EMBO J., vol. 11, no. 4, p. 1469–1477, 1992, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Acute-Phase Proteins, Adipose Tissue, Animals, Base Sequence, beta-Galactosidase, Embryo, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Mammals, Nonmammalian, Oligodeoxyribonucleotides, Promoter Regions, Recombinant Fusion Proteins, reichhart, Restriction Mapping
@article{reichhart_insect_1992,
title = {Insect immunity: developmental and inducible activity of the Drosophila diptericin promoter},
author = {Jean-Marc Reichhart and Marie Meister and Jean-Luc Dimarcq and Daniel Zachary and Danièle Hoffmann and C Ruiz and G Richards and Jules A Hoffmann},
issn = {0261-4189},
year = {1992},
date = {1992-01-01},
journal = {EMBO J.},
volume = {11},
number = {4},
pages = {1469--1477},
abstract = {Diptericins are 9 kDa inducible antibacterial peptides initially isolated from immune haemolymph of Phormia (Diptera). Following the isolation of a Drosophila cDNA encoding a diptericin homologue, we have now cloned a genomic fragment containing the Drosophila diptericin gene. To dissect the regulation of this gene, we have transformed flies with a fusion gene in which the reporter beta-galactosidase gene is under the control of 2.2 kb upstream sequences of the diptericin gene. We show that such a fusion gene is inducible by injection of live bacteria or complete Freund's adjuvant and respects the tissue specific expression pattern of the resident diptericin gene. Our analysis reveals at least four distinct phases in the regulation of this gene: young larvae, late third instar larvae, pupae and adults. This complexity may be related to the presence in the upstream sequences of multiple copies of response elements previously characterized in genes encoding acute phase response proteins in mammals (e.g. NK-kappa B, NF-kappa B related, NF-IL6 response elements).},
keywords = {Acute-Phase Proteins, Adipose Tissue, Animals, Base Sequence, beta-Galactosidase, Embryo, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Mammals, Nonmammalian, Oligodeoxyribonucleotides, Promoter Regions, Recombinant Fusion Proteins, reichhart, Restriction Mapping},
pubstate = {published},
tppubtype = {article}
}
Bonmatin J M, Bonnat J L, Gallet X, Vovelle F, Ptak M, Reichhart Jean-Marc, Hoffmann Jules A, Keppi E, Legrain M, Achstetter T
Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding Article de journal
Dans: J. Biomol. NMR, vol. 2, no. 3, p. 235–256, 1992, ISSN: 0925-2738.
Résumé | BibTeX | Étiquettes: Animals, Defensins, hoffmann, Hydrogen, Insect Hormones, insects, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Recombinant Proteins, reichhart, Saccharomyces cerevisiae, Thermodynamics
@article{bonmatin_two-dimensional_1992,
title = {Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding},
author = {J M Bonmatin and J L Bonnat and X Gallet and F Vovelle and M Ptak and Jean-Marc Reichhart and Jules A Hoffmann and E Keppi and M Legrain and T Achstetter},
issn = {0925-2738},
year = {1992},
date = {1992-01-01},
journal = {J. Biomol. NMR},
volume = {2},
number = {3},
pages = {235--256},
abstract = {A 500 MHz 2D 1H NMR study of recombinant insect defensin A is reported. This defense protein of 40 residues contains 3 disulfide bridges, is positively charged and exhibits antibacterial properties. 2D NMR maps of recombinant defensin A were fully assigned and secondary structure elements were localized. The set of NOE connectivities, 3JNH-alpha H coupling constants as well as 1H/2H exchange rates and delta delta/delta T temperature coefficients of NH protons strongly support the existence of an alpha-helix (residues 14-24) and of an antiparallel beta-sheet (residues 27-40). Models of the backbone folding were generated by using the DISMAN program and energy refined by using the AMBER program. This was done on the basis of: (i) 133 selected NOEs, (ii) 21 dihedral restraints from 3JNH-alpha H coupling constants, (iii) 12 hydrogen bonds mostly deduced from 1H/2H exchange rates or temperature coefficients, in addition to 9 initial disulfide bridge covalent constraints. The two secondary structure elements and the two bends connecting them involve approximately 70% of the total number of residues, which impose some stability in the C-terminal part of the molecule. The remaining N-terminal fragment forms a less well defined loop. This spatial organization, in which a beta-sheet is linked to an alpha-helix by two disulfide bridges and to a large loop by a third disulfide bridge, is rather similar to that found in scorpion charybdotoxin and seems to be partly present in several invertebrate toxins.},
keywords = {Animals, Defensins, hoffmann, Hydrogen, Insect Hormones, insects, M3i, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Recombinant Proteins, reichhart, Saccharomyces cerevisiae, Thermodynamics},
pubstate = {published},
tppubtype = {article}
}
Bulet Philippe, Cociancich S, Dimarcq Jean-Luc, Lambert J, Reichhart Jean-Marc, Hoffmann Danièle, Hetru Charles, Hoffmann Jules A
Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family Article de journal
Dans: J. Biol. Chem., vol. 266, no. 36, p. 24520–24525, 1991, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Antibody Formation, Beetles, Blood Bactericidal Activity, Blood Proteins, Chromatography, Defensins, Hemolymph, High Pressure Liquid, hoffmann, Insect Hormones, Insect Proteins, M3i, reichhart
@article{bulet_insect_1991,
title = {Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family},
author = {Philippe Bulet and S Cociancich and Jean-Luc Dimarcq and J Lambert and Jean-Marc Reichhart and Danièle Hoffmann and Charles Hetru and Jules A Hoffmann},
issn = {0021-9258},
year = {1991},
date = {1991-12-01},
journal = {J. Biol. Chem.},
volume = {266},
number = {36},
pages = {24520--24525},
abstract = {Injection of heat-killed bacteria into larvae of the large tenebrionid beetle Zophobas atratus (Insecta, Endopterygota, Coleoptera) results in the appearance in the hemolymph of a potent antibacterial activity as evidenced by a plate growth inhibition assay. We have isolated three peptides (A-C) from this immune hemolymph which probably account for most of this activity. Their primary structures were established by a combination of peptide sequencing and molecular mass determination by mass spectrometry. Peptide A, which is bactericidal against Gram-negative cells, is a 74-residue glycine-rich molecule with no sequence homology to known peptides. We propose the name coleoptericin for this novel inducible antibacterial peptide. Peptides B and C are isoforms of a 43-residue peptide which contains 6 cysteines and shows significant sequence homology to insect defensins, initially reported from dipteran insects. This peptide is active against Gram-positive bacteria. The results are discussed in connection with recent studies on inducible antibacterial peptides present in the three other major orders of the endopterygote clade of insects: the Lepidoptera, Diptera, and Hymenoptera.},
keywords = {Animals, Antibody Formation, Beetles, Blood Bactericidal Activity, Blood Proteins, Chromatography, Defensins, Hemolymph, High Pressure Liquid, hoffmann, Insect Hormones, Insect Proteins, M3i, reichhart},
pubstate = {published},
tppubtype = {article}
}
Hetru Charles, Li K W, Bulet Philippe, Lagueux Marie, Hoffmann Jules A
Isolation and structural characterization of an insulin-related molecule, a predominant neuropeptide from Locusta migratoria Article de journal
Dans: Eur. J. Biochem., vol. 201, no. 2, p. 495–499, 1991, ISSN: 0014-2956.
Résumé | BibTeX | Étiquettes: Animals, Chromatography, DNA, Female, Grasshoppers, High Pressure Liquid, hoffmann, Insect Hormones, Insulin, M3i, Mass Spectrometry, Neuropeptides, Proinsulin, Protein Conformation
@article{hetru_isolation_1991,
title = {Isolation and structural characterization of an insulin-related molecule, a predominant neuropeptide from Locusta migratoria},
author = {Charles Hetru and K W Li and Philippe Bulet and Marie Lagueux and Jules A Hoffmann},
issn = {0014-2956},
year = {1991},
date = {1991-10-01},
journal = {Eur. J. Biochem.},
volume = {201},
number = {2},
pages = {495--499},
abstract = {Neurohaemal lobes of corpora cardiaca of Locusta migratoria are an established storage site for neurohormones produced by the neurosecretory cells of the brain. As previously reported [Hietter, H., Van Dorsselaer, A., Green, B., Denoroy, L., Hoffmann, J.A. & Luu, B. (1990) Eur. J. Biochem. 187, 241-247], the isolation and characterization of a novel 5-kDa peptide from these lobes served as the basis for oligonucleotide screening of cDNA libraries prepared from poly(A) RNA from neurosecretory cells of the central nervous system. From subsequent cDNA cloning studies [Lagueux, M., Lwoff, L., Meister, M., Goltzené, F. & Hoffmann, J.A. (1990) Eur. J. Biochem. 187, 249-254], the existence of a 145-residue precursor protein was deduced, which contained, in addition to the 5-kDa peptide, amino-acid sequences with homology to the A and B chains of an insulin-related peptide. In the present study we have isolated the native molecule from corpora cardiaca of Locusta and characterized, by Edman degradation and plasma-desorption mass spectrometry, the two chains as follows: A chain, Gly-Val-Phe-Asp-Glu-Cys-Cys-Arg-Lys-Ser-Cys-Ser-Ile-Ser-Glu-Leu-Gln-Thr- Tyr-Cys - Gly (Ile, isoleucine); B chain, Ser-Gly-Ala-Pro-Gln-Pro-Val-Ala-Arg-Tyr-Cys-Gly-Glu-Lys-Leu-Ser-Asn-Ala- Leu-Lys - Leu-Val-Cys-Arg-Gly-Asn-Tyr-Asn-Thr-Met-Phe. Taken in conjunction with the previous cloning studies, our data lead to a clear picture of the processing of Locusta preproinsulin. They indicate that locusta corpora cardiaca contain remarkably large amounts of one single insulin form, in contrast to multiple insulin isoforms of Bombyx mori, the only other insect species from which insulin-related peptides have been isolated and characterized [Nagasawa, H., Kataoka, H., Isogai, A., Tamura, S., Suzuki, A., Mizoguchi, A., Fujiwara, Y., Suzuki, A., Takahashi, S. & Ishizaki, H. (1986) Proc. Natl Acad. Sci. USA 83, 5840-5843].},
keywords = {Animals, Chromatography, DNA, Female, Grasshoppers, High Pressure Liquid, hoffmann, Insect Hormones, Insulin, M3i, Mass Spectrometry, Neuropeptides, Proinsulin, Protein Conformation},
pubstate = {published},
tppubtype = {article}
}
Hoffmann Jules A, Hoffmann Danièle
The inducible antibacterial peptides of dipteran insects Article de journal
Dans: Res. Immunol., vol. 141, no. 9, p. 910–918, 1990, ISSN: 0923-2494.
BibTeX | Étiquettes: Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription
@article{hoffmann_inducible_1990,
title = {The inducible antibacterial peptides of dipteran insects},
author = {Jules A Hoffmann and Danièle Hoffmann},
issn = {0923-2494},
year = {1990},
date = {1990-12-01},
journal = {Res. Immunol.},
volume = {141},
number = {9},
pages = {910--918},
keywords = {Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription},
pubstate = {published},
tppubtype = {article}
}
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}
}
Hetru Charles, Luu B, Hoffmann Jules A
Ecdysone conjugates: isolation and identification Article de journal
Dans: Meth. Enzymol., vol. 111, p. 411–419, 1985, ISSN: 0076-6879.
BibTeX | Étiquettes: Animals, Bombyx, Chromatography, Ecdysone, Helix (Snails), High Pressure Liquid, hoffmann, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Spectrophotometry, Structure-Activity Relationship
@article{hetru_ecdysone_1985,
title = {Ecdysone conjugates: isolation and identification},
author = {Charles Hetru and B Luu and Jules A Hoffmann},
issn = {0076-6879},
year = {1985},
date = {1985-01-01},
journal = {Meth. Enzymol.},
volume = {111},
pages = {411--419},
keywords = {Animals, Bombyx, Chromatography, Ecdysone, Helix (Snails), High Pressure Liquid, hoffmann, Insect Hormones, M3i, Magnetic Resonance Spectroscopy, Mass Spectrometry, Spectrophotometry, Structure-Activity Relationship},
pubstate = {published},
tppubtype = {article}
}