Limmer Stefanie, Quintin Jessica, Hetru Charles, Ferrandon Dominique
Virulence on the fly: Drosophila melanogaster as a model genetic organism to decipher host-pathogen interactions Article de journal
Dans: Curr Drug Targets, vol. 12, no. 7, p. 978–999, 2011, ISSN: 1873-5592.
Résumé | BibTeX | Étiquettes: Animal, Animals, Anti-Infective Agents, Disease Models, Drug Delivery Systems, Drug Design, Drug Resistance, ferrandon, Fungi, High-Throughput Screening Assays, Host-Pathogen Interactions, Humans, M3i, Microbial, Pseudomonas aeruginosa
@article{limmer_virulence_2011b,
title = {Virulence on the fly: Drosophila melanogaster as a model genetic organism to decipher host-pathogen interactions},
author = {Stefanie Limmer and Jessica Quintin and Charles Hetru and Dominique Ferrandon},
issn = {1873-5592},
year = {2011},
date = {2011-06-01},
journal = {Curr Drug Targets},
volume = {12},
number = {7},
pages = {978--999},
abstract = {To gain an in-depth grasp of infectious processes one has to know the specific interactions between the virulence factors of the pathogen and the host defense mechanisms. A thorough understanding is crucial for identifying potential new drug targets and designing drugs against which the pathogens might not develop resistance easily. Model organisms are a useful tool for this endeavor, thanks to the power of their genetics. Drosophila melanogaster is widely used to study host-pathogen interactions. Its basal immune response is well understood and is briefly reviewed here. Considerations relevant to choosing an adequate infection model are discussed. This review then focuses mainly on infections with two categories of pathogens, the well-studied Gram-negative bacterium Pseudomonas aeruginosa and infections by fungi of medical interest. These examples provide an overview over the current knowledge on Drosophila-pathogen interactions and illustrate the approaches that can be used to study those interactions. We also discuss the usefulness and limits of Drosophila infection models for studying specific host-pathogen interactions and high-throughput drug screening.},
keywords = {Animal, Animals, Anti-Infective Agents, Disease Models, Drug Delivery Systems, Drug Design, Drug Resistance, ferrandon, Fungi, High-Throughput Screening Assays, Host-Pathogen Interactions, Humans, M3i, Microbial, Pseudomonas aeruginosa},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Bianco Alberto, Pellarini Federica, Tossi Alessandro, Giangaspero Anna, Zelezetsky Igor, Briand Jean-Paul, Prato Maurizio
Solid-phase synthesis of fullerene-peptides Article de journal
Dans: Journal of the American Chemical Society, vol. 124, no. 42, p. 12543–12549, 2002, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco
@article{pantarotto_solid-phase_2002,
title = {Solid-phase synthesis of fullerene-peptides},
author = {Davide Pantarotto and Alberto Bianco and Federica Pellarini and Alessandro Tossi and Anna Giangaspero and Igor Zelezetsky and Jean-Paul Briand and Maurizio Prato},
doi = {10.1021/ja027603q},
issn = {0002-7863},
year = {2002},
date = {2002-10-01},
journal = {Journal of the American Chemical Society},
volume = {124},
number = {42},
pages = {12543--12549},
abstract = {The solid-phase synthesis of peptides (SPPS) containing [60]fullerene-functionalized amino acids is reported. A new amino acid, fulleropyrrolidino-glutamic acid (Fgu), is used for the SPPS of a series of analogues of different length based on the natural Leu(5)-Enkephalin and on cationic antimicrobial peptides. These fullero-peptides were prepared on different solid supports to analyze the influence of the resin on the synthesis. Optimized protocols for the coupling and deprotection procedures were determined allowing the synthesis of highly pure peptides in sufficient quantities for evaluation of biological activities. In particular, to avoid side reactions of the fullerene moiety with bases and nucleophiles, the removal of the protecting groups was performed under inert conditions (nitrogen or argon in the dark). We have encountered serious problems with the recovery of the crude compounds, especially when Fgu was inserted in the proximity of the resin core as fullero-peptides tend to remain embedded inside the resin. Eventually, all of the fullero-peptides were easily purified, and the cationic peptides were tested for their antimicrobial activities. They displayed a specific activity against the Gram-positive bacterium S. aureus and also lysed erythrocytes. The availability of a fullero-amino acid easily useable in the SPPS of fullero-peptides may thus open the way to the synthesis of new types of biologically active oligomers.},
keywords = {Amino Acids, Anti-Bacterial Agents, Anti-Infective Agents, Candida albicans, Electrospray Ionization, Enkephalin, Escherichia coli, Fluorenes, Fullerenes, I2CT, Leucine, Mass, Microbial Sensitivity Tests, Oligopeptides, Spectrometry, Staphylococcus aureus, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Michel T, Reichhart Jean-Marc, Hoffmann Jules A, Royet Julien
Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein Article de journal
Dans: Nature, vol. 414, no. 6865, p. 756–759, 2001, ISSN: 0028-0836.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Bacillus thuringiensis, Carrier Proteins, Cell Surface, Chromosome Mapping, Enterococcus faecalis, Fungi, Genes, Gram-Positive Bacteria, Hemolymph, hoffmann, Humans, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutation, Receptors, reichhart, Sequence Homology, Toll-Like Receptors
@article{michel_drosophila_2001,
title = {Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein},
author = {T Michel and Jean-Marc Reichhart and Jules A Hoffmann and Julien Royet},
doi = {10.1038/414756a},
issn = {0028-0836},
year = {2001},
date = {2001-12-01},
journal = {Nature},
volume = {414},
number = {6865},
pages = {756--759},
abstract = {Microbial infection activates two distinct intracellular signalling cascades in the immune-responsive fat body of Drosophila. Gram-positive bacteria and fungi predominantly induce the Toll signalling pathway, whereas Gram-negative bacteria activate the Imd pathway. Loss-of-function mutants in either pathway reduce the resistance to corresponding infections. Genetic screens have identified a range of genes involved in these intracellular signalling cascades, but how they are activated by microbial infection is largely unknown. Activation of the transmembrane receptor Toll requires a proteolytically cleaved form of an extracellular cytokine-like polypeptide, Spätzle, suggesting that Toll does not itself function as a bona fide recognition receptor of microbial patterns. This is in apparent contrast with the mammalian Toll-like receptors and raises the question of which host molecules actually recognize microbial patterns to activate Toll through Spätzle. Here we present a mutation that blocks Toll activation by Gram-positive bacteria and significantly decreases resistance to this type of infection. The mutation semmelweis (seml) inactivates the gene encoding a peptidoglycan recognition protein (PGRP-SA). Interestingly, seml does not affect Toll activation by fungal infection, indicating the existence of a distinct recognition system for fungi to activate the Toll pathway.},
keywords = {Amino Acid, Animals, Anti-Bacterial Agents, Anti-Infective Agents, Bacillus thuringiensis, Carrier Proteins, Cell Surface, Chromosome Mapping, Enterococcus faecalis, Fungi, Genes, Gram-Positive Bacteria, Hemolymph, hoffmann, Humans, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Micrococcus luteus, Mutation, Receptors, reichhart, Sequence Homology, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Georgel Philippe, Naitza S, Kappler Christine, Ferrandon Dominique, Zachary Daniel, Swimmer C, Kopczynski C, Duyk G, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis Article de journal
Dans: Dev. Cell, vol. 1, no. 4, p. 503–514, 2001, ISSN: 1534-5807.
Résumé | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary
@article{georgel_drosophila_2001,
title = {Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis},
author = {Philippe Georgel and S Naitza and Christine Kappler and Dominique Ferrandon and Daniel Zachary and C Swimmer and C Kopczynski and G Duyk and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {1534-5807},
year = {2001},
date = {2001-10-01},
journal = {Dev. Cell},
volume = {1},
number = {4},
pages = {503--514},
abstract = {We report the molecular characterization of the immune deficiency (imd) gene, which controls antibacterial defense in Drosophila. imd encodes a protein with a death domain similar to that of mammalian RIP (receptor interacting protein), a protein that plays a role in both NF-kappaB activation and apoptosis. We show that imd functions upstream of the DmIKK signalosome and the caspase DREDD in the control of antibacterial peptide genes. Strikingly, overexpression of imd leads to constitutive transcription of these genes and to apoptosis, and both effects are blocked by coexpression of the caspase inhibitor P35. We also show that imd is involved in the apoptotic response to UV irradiation. These data raise the possibility that antibacterial response and apoptosis share common control elements in Drosophila.},
keywords = {Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary},
pubstate = {published},
tppubtype = {article}
}
Vizioli J, Bulet Philippe, Hoffmann Jules A, Kafatos Fotis C, Müller H M, Dimopoulos G
Gambicin: a novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae Article de journal
Dans: Proc. Natl. Acad. Sci. U.S.A., vol. 98, no. 22, p. 12630–12635, 2001, ISSN: 0027-8424.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anopheles, Anti-Bacterial Agents, Anti-Infective Agents, Base Sequence, Chromosome Mapping, hoffmann, Insect Proteins, Insect Vectors, M3i, Malaria, messenger, RNA
@article{vizioli_gambicin:_2001,
title = {Gambicin: a novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae},
author = {J Vizioli and Philippe Bulet and Jules A Hoffmann and Fotis C Kafatos and H M Müller and G Dimopoulos},
doi = {10.1073/pnas.221466798},
issn = {0027-8424},
year = {2001},
date = {2001-10-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {98},
number = {22},
pages = {12630--12635},
abstract = {A novel mosquito antimicrobial peptide, gambicin, and the corresponding gene were isolated in parallel through differential display-PCR, an expressed sequence tag (EST) project, and characterization of an antimicrobial activity in a mosquito cell line by reverse-phase chromatography. The 616-bp gambicin ORF encodes an 81-residue protein that is processed and secreted as a 61-aa mature peptide containing eight cysteines engaged in four disulfide bridges. Gambicin lacks sequence homology with other known proteins. Like other Anopheles gambiae antimicrobial peptide genes, gambicin is induced by natural or experimental infection in the midgut, fatbody, and hemocyte-like cell lines. Within the midgut, gambicin is predominantly expressed in the anterior part. Both local and systemic gambicin expression is induced during early and late stages of natural malaria infection. In vitro experiments showed that the 6.8-kDa mature peptide can kill both Gram-positive and Gram-negative bacteria, has a morphogenic effect on a filamentous fungus, and is marginally lethal to Plasmodium berghei ookinetes. An oxidized form of gambicin isolated from the cell line medium was more active against bacteria than the nonoxidized form from the same medium.},
keywords = {Animals, Anopheles, Anti-Bacterial Agents, Anti-Infective Agents, Base Sequence, Chromosome Mapping, hoffmann, Insect Proteins, Insect Vectors, M3i, Malaria, messenger, RNA},
pubstate = {published},
tppubtype = {article}
}
Imler Jean-Luc, Hoffmann Jules A
Signaling mechanisms in the antimicrobial host defense of Drosophila Article de journal
Dans: Current Opinion in Microbiology, vol. 3, no. 1, p. 16–22, 2000, ISSN: 1369-5274.
Résumé | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Cell Surface, Gene Expression Regulation, Genes, hoffmann, imler, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Receptors, Signal Transduction, Toll-Like Receptors
@article{imler_signaling_2000,
title = {Signaling mechanisms in the antimicrobial host defense of Drosophila},
author = {Jean-Luc Imler and Jules A Hoffmann},
issn = {1369-5274},
year = {2000},
date = {2000-02-01},
journal = {Current Opinion in Microbiology},
volume = {3},
number = {1},
pages = {16--22},
abstract = {Drosophila has appeared in recent years as a powerful model to study innate immunity. Several papers published in the past year shed light on the role of the three Rel proteins Dorsal, Dif and Relish in the regulation of antimicrobial peptide expression. In addition, the discovery that a blood serine protease inhibitor is involved in the control of the antifungal response indicates that Toll is activated upon triggering of a proteolytic cascade and does not function as a Drosophila pattern recognition receptor.},
keywords = {Animals, Anti-Infective Agents, Cell Surface, Gene Expression Regulation, Genes, hoffmann, imler, Insect, Insect Proteins, M3i, Membrane Glycoproteins, Receptors, Signal Transduction, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Meister Marie, Hetru Charles, Hoffmann Jules A
The antimicrobial host defense of Drosophila Article de journal
Dans: Curr. Top. Microbiol. Immunol., vol. 248, p. 17–36, 2000, ISSN: 0070-217X.
BibTeX | Étiquettes: Animals, Anti-Infective Agents, Fat Body, Genes, hoffmann, Insect, Insect Proteins, M3i
@article{meister_antimicrobial_2000,
title = {The antimicrobial host defense of Drosophila},
author = {Marie Meister and Charles Hetru and Jules A Hoffmann},
issn = {0070-217X},
year = {2000},
date = {2000-01-01},
journal = {Curr. Top. Microbiol. Immunol.},
volume = {248},
pages = {17--36},
keywords = {Animals, Anti-Infective Agents, Fat Body, Genes, hoffmann, Insect, Insect Proteins, M3i},
pubstate = {published},
tppubtype = {article}
}
Manfruelli P, Reichhart Jean-Marc, Steward R, Hoffmann Jules A, Lemaitre Bruno
A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF Article de journal
Dans: EMBO J., vol. 18, no. 12, p. 3380–3391, 1999, ISSN: 0261-4189.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Cell Surface, Clone Cells, DNA-Binding Proteins, Fat Body, Female, Gene Expression Regulation, Genes, hoffmann, Insect, Insect Proteins, Larva, M3i, Male, Membrane Glycoproteins, Mosaicism, Mutation, Nuclear Proteins, Phosphoproteins, Receptors, reichhart, Reporter, Signal Transduction, Toll-Like Receptors, Transcription Factors
@article{manfruelli_mosaic_1999,
title = {A mosaic analysis in Drosophila fat body cells of the control of antimicrobial peptide genes by the Rel proteins Dorsal and DIF},
author = {P Manfruelli and Jean-Marc Reichhart and R Steward and Jules A Hoffmann and Bruno Lemaitre},
doi = {10.1093/emboj/18.12.3380},
issn = {0261-4189},
year = {1999},
date = {1999-06-01},
journal = {EMBO J.},
volume = {18},
number = {12},
pages = {3380--3391},
abstract = {Expression of the gene encoding the antifungal peptide Drosomycin in Drosophila adults is controlled by the Toll signaling pathway. The Rel proteins Dorsal and DIF (Dorsal-related immunity factor) are possible candidates for the transactivating protein in the Toll pathway that directly regulates the drosomycin gene. We have examined the requirement of Dorsal and DIF for drosomycin expression in larval fat body cells, the predominant immune-responsive tissue, using the yeast site-specific flp/FRT recombination system to generate cell clones homozygous for a deficiency uncovering both the dorsal and the dif genes. Here we show that in the absence of both genes, the immune-inducibility of drosomycin is lost but can be rescued by overexpression of either dorsal or dif under the control of a heat-shock promoter. This result suggests a functional redundancy between both Rel proteins in the control of drosomycin gene expression in the larvae of Drosophila. Interestingly, the gene encoding the antibacterial peptide Diptericin remains fully inducible in the absence of the dorsal and dif genes. Finally, we have used fat body cell clones homozygous for various mutations to show that a linear activation cascade Spaetzle--textgreater Toll--textgreaterCactus--textgreaterDorsal/DIF leads to the induction of the drosomycin gene in larval fat body cells.},
keywords = {Animals, Anti-Infective Agents, Cell Surface, Clone Cells, DNA-Binding Proteins, Fat Body, Female, Gene Expression Regulation, Genes, hoffmann, Insect, Insect Proteins, Larva, M3i, Male, Membrane Glycoproteins, Mosaicism, Mutation, Nuclear Proteins, Phosphoproteins, Receptors, reichhart, Reporter, Signal Transduction, Toll-Like Receptors, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Bulet Philippe, Uttenweiler-Joseph S, Moniatte M, Dorsselaer Van A, Hoffmann Jules A
Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study Article de journal
Dans: J. Protein Chem., vol. 17, no. 6, p. 528–529, 1998, ISSN: 0277-8033.
BibTeX | Étiquettes: Animals, Anti-Infective Agents, hoffmann, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Peptide Biosynthesis, Peptides, Spectrometry
@article{bulet_differential_1998,
title = {Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study},
author = {Philippe Bulet and S Uttenweiler-Joseph and M Moniatte and Van A Dorsselaer and Jules A Hoffmann},
issn = {0277-8033},
year = {1998},
date = {1998-08-01},
journal = {J. Protein Chem.},
volume = {17},
number = {6},
pages = {528--529},
keywords = {Animals, Anti-Infective Agents, hoffmann, M3i, Mass, Matrix-Assisted Laser Desorption-Ionization, Peptide Biosynthesis, Peptides, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Shahabuddin M, Fields I, Bulet Philippe, Hoffmann Jules A, Miller L H
Plasmodium gallinaceum: differential killing of some mosquito stages of the parasite by insect defensin Article de journal
Dans: Exp. Parasitol., vol. 89, no. 1, p. 103–112, 1998, ISSN: 0014-4894.
Résumé | Liens | BibTeX | Étiquettes: Aedes, Animals, Anti-Infective Agents, Blood Proteins, Defensins, Diptera, hoffmann, Insect Vectors, insects, M3i, Plasmodium gallinaceum, Zygote
@article{shahabuddin_plasmodium_1998,
title = {Plasmodium gallinaceum: differential killing of some mosquito stages of the parasite by insect defensin},
author = {M Shahabuddin and I Fields and Philippe Bulet and Jules A Hoffmann and L H Miller},
doi = {10.1006/expr.1998.4212},
issn = {0014-4894},
year = {1998},
date = {1998-05-01},
journal = {Exp. Parasitol.},
volume = {89},
number = {1},
pages = {103--112},
abstract = {We examined several insect antimicrobial peptides to study their effect on Plasmodium gallinaceum zygotes, ookinetes, oocysts, and sporozoites. Only two insect defensins-Aeschna cyanea (dragon fly) and Phormia terranovae (flesh fly)-had a profound toxic effect on the oocysts in Aedes aegypti and on isolated sporozoites. The defensins affected the oocysts in a time-dependent manner. Injecting the peptide into the hemolymph 1 or 2 days after an infectious blood meal had no significant effect on prevalence of infection or relative oocyst density per mosquito. When injected 3 days after parasite ingestion, the relative oocyst density was significantly reduced. Injection on day 4 or later damaged the developing oocysts, although the oocysts density per mosquito was not significantly different when examined on day 8. The oocysts were swollen or had extensive internal vacuolization. The peptides had no detectable effect on the early stages of the parasite: the zygotes and ookinetes tested in vitro. Both the defensins were highly toxic to isolated sporozoites in vitro as indicated by disruption of the membrane permeability barrier, a change in morphology, and loss of motility. In contrast to the toxicity of cecropin and magainin for mosquitoes, defensin, at concentrations that kill parasites, is not toxic to mosquitoes, suggesting that defensin should be studied further as a potential molecule to block sporogonic development of Plasmodium.},
keywords = {Aedes, Animals, Anti-Infective Agents, Blood Proteins, Defensins, Diptera, hoffmann, Insect Vectors, insects, M3i, Plasmodium gallinaceum, Zygote},
pubstate = {published},
tppubtype = {article}
}
Levashina Elena A, Ohresser S, Lemaitre Bruno, Imler Jean-Luc
Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin Article de journal
Dans: Journal of Molecular Biology, vol. 278, no. 3, p. 515–527, 1998, ISSN: 0022-2836.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Antimicrobial Cationic Peptides, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Glycopeptides, imler, Insect, Insect Proteins, Larva, M3i, Molecular, Mutation, Peptides, Promoter Regions, Recombinant Fusion Proteins, Reporter, Restriction Mapping, Transcription
@article{levashina_two_1998,
title = {Two distinct pathways can control expression of the gene encoding the Drosophila antimicrobial peptide metchnikowin},
author = {Elena A Levashina and S Ohresser and Bruno Lemaitre and Jean-Luc Imler},
doi = {10.1006/jmbi.1998.1705},
issn = {0022-2836},
year = {1998},
date = {1998-01-01},
journal = {Journal of Molecular Biology},
volume = {278},
number = {3},
pages = {515--527},
abstract = {Metchnikowin is a recently discovered proline-rich peptide from Drosophila with antibacterial and antifungal properties. Like most other antimicrobial peptides from insects, its expression is immune-inducible. Here we present evidence that induction of metchnikowin gene expression can be mediated either by the TOLL pathway or by the imd gene product. We show that the gene remains inducible in Toll-deficient mutants, in which the antifungal response is blocked, as well as in imd mutants, which fail to mount an antibacterial response. However, in Toll-deficient;imd double mutants, metchnikowin gene expression can no longer be detected after immune challenge. Our results suggest that expression of this peptide with dual activity can be triggered by signals generated by either bacterial or fungal infection. Cloning of the metchnikowin gene revealed the presence in the 5' flanking region of several putative cis-regulatory motifs characterized in the promoters of insect immune genes: namely, Rel sites, GATA motifs, interferon consensus response elements and NF-IL6 response elements. Establishment of transgenic fly lines in which the GFP reporter gene was placed under the control of 1.5 kb of metchnikowin gene upstream sequences indicates that this fragment is able to confer full immune inducibility and tissue specificity of expression on the transgene.},
keywords = {Animals, Anti-Infective Agents, Antimicrobial Cationic Peptides, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Glycopeptides, imler, Insect, Insect Proteins, Larva, M3i, Molecular, Mutation, Peptides, Promoter Regions, Recombinant Fusion Proteins, Reporter, Restriction Mapping, Transcription},
pubstate = {published},
tppubtype = {article}
}
Meister Marie, Lemaitre Bruno, Hoffmann Jules A
Antimicrobial peptide defense in Drosophila Article de journal
Dans: Bioessays, vol. 19, no. 11, p. 1019–1026, 1997, ISSN: 0265-9247.
Résumé | Liens | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Gene Expression Regulation, Genetic, hoffmann, Insect Proteins, M3i, Models, Peptides, Promoter Regions, Signal Transduction
@article{meister_antimicrobial_1997,
title = {Antimicrobial peptide defense in Drosophila},
author = {Marie Meister and Bruno Lemaitre and Jules A Hoffmann},
doi = {10.1002/bies.950191112},
issn = {0265-9247},
year = {1997},
date = {1997-11-01},
journal = {Bioessays},
volume = {19},
number = {11},
pages = {1019--1026},
abstract = {Drosophila responds to a septic injury by the rapid synthesis of antimicrobial peptides. These molecules are predominantly produced by the fat body, a functional equivalent of mammalian liver, and are secreted into the hemolymph where their concentrations can reach up to 100 microM. Six distinct antibacterial peptides (plus isoforms) and one antifungal peptide have been characterized in Drosophila and their genes cloned. The induction of the gene encoding the antifungal peptide relies on the spätzle/Toll/cactus gene cassette, which is involved in the control of dorsoventral patterning in the embryo, and shows interesting structural and functional similarities with cytokine-induced activation of NF-kappa B in mammalian cells. An additional pathway, dependent on the as yet unidentified imd (for immune-deficiency) gene, is required for the full induction of the antibacterial peptide genes. Mutants deficient for the Toll and imd pathways exhibit a severely reduced survival to fungal and bacterial infections, respectively. Recent data on the molecular mechanisms underlying recognition of non-self are also discussed in this review.},
keywords = {Animals, Anti-Infective Agents, Gene Expression Regulation, Genetic, hoffmann, Insect Proteins, M3i, Models, Peptides, Promoter Regions, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Charlet Maurice, Chernysh S, Philippe H, Hetru Charles, Hoffmann Jules A, Bulet Philippe
Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis Article de journal
Dans: J. Biol. Chem., vol. 271, no. 36, p. 21808–21813, 1996, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology
@article{charlet_innate_1996,
title = {Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis},
author = {Maurice Charlet and S Chernysh and H Philippe and Charles Hetru and Jules A Hoffmann and Philippe Bulet},
issn = {0021-9258},
year = {1996},
date = {1996-09-01},
journal = {J. Biol. Chem.},
volume = {271},
number = {36},
pages = {21808--21813},
abstract = {We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.},
keywords = {Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
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}
}
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}
}
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}
}