Prakash Pragya, Roychowdhury-Sinha Arghyashree, Goto Akira
Verloren negatively regulates the expression of IMD pathway dependent antimicrobial peptides in Drosophila Article de journal
Dans: Scientific Reports, vol. 11, no. 15549, 2021.
Résumé | Liens | BibTeX | Étiquettes: bacteria, Biochemistry, DNA, Fungi, Gene Expression, gene regulation, Genetics, hoffmann, Immunochemistry, Immunology, infection, inflammation, Innate immune cells, innate immunity, M3i, microbiology, Molecular Biology, pathogens, RNA, RNAi, Signal Transduction, Transcription
@article{Goto2021,
title = {Verloren negatively regulates the expression of IMD pathway dependent antimicrobial peptides in Drosophila},
author = {Pragya Prakash and Arghyashree Roychowdhury-Sinha and Akira Goto},
url = {https://www.nature.com/articles/s41598-021-94973-0},
doi = {10.1038/s41598-021-94973-0},
year = {2021},
date = {2021-07-30},
journal = {Scientific Reports},
volume = {11},
number = {15549},
abstract = {Drosophila immune deficiency (IMD) pathway is similar to the human tumor necrosis factor receptor (TNFR) signaling pathway and is preferentially activated by Gram-negative bacterial infection. Recent studies highlighted the importance of IMD pathway regulation as it is tightly controlled by numbers of negative regulators at multiple levels. Here, we report a new negative regulator of the IMD pathway, Verloren (Velo). Silencing of Velo led to constitutive expression of the IMD pathway dependent antimicrobial peptides (AMPs), and Escherichia coli stimulation further enhanced the AMP expression. Epistatic analysis indicated that Velo knock-down mediated AMP upregulation is dependent on the canonical members of the IMD pathway. The immune fluorescent study using overexpression constructs revealed that Velo resides both in the nucleus and cytoplasm, but the majority (~ 75%) is localized in the nucleus. We also observed from in vivo analysis that Velo knock-down flies exhibit significant upregulation of the AMP expression and reduced bacterial load. Survival experiments showed that Velo knock-down flies have a short lifespan and are susceptible to the infection of pathogenic Gram-negative bacteria, P. aeruginosa. Taken together, these data suggest that Velo is an additional new negative regulator of the IMD pathway, possibly acting in both the nucleus and cytoplasm.},
keywords = {bacteria, Biochemistry, DNA, Fungi, Gene Expression, gene regulation, Genetics, hoffmann, Immunochemistry, Immunology, infection, inflammation, Innate immune cells, innate immunity, M3i, microbiology, Molecular Biology, pathogens, RNA, RNAi, Signal Transduction, Transcription},
pubstate = {published},
tppubtype = {article}
}
Patrnogic Jelena, Leclerc Vincent
The serine protease homolog spheroide is involved in sensing of pathogenic Gram-positive bacteria Article de journal
Dans: PLoS One, vol. 12, no. 12, 2017.
Résumé | Liens | BibTeX | Étiquettes: Fungi, Gram-Positive Bacteria, serine protease, spheroide, toll pathway
@article{Jelena2017,
title = {The serine protease homolog spheroide is involved in sensing of pathogenic Gram-positive bacteria},
author = {Jelena Patrnogic and Vincent Leclerc},
url = {https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5718610/},
doi = {10.1371/journal.pone.0188339},
year = {2017},
date = {2017-12-06},
journal = {PLoS One},
volume = {12},
number = {12},
abstract = {In Drosophila, recognition of pathogens such as Gram-positive bacteria and fungi triggers the activation of proteolytic cascades and the subsequent activation of the Toll pathway. This response can be achieved by either detection of pathogen associated molecular patterns or by sensing microbial proteolytic activities ("danger signals"). Previous data suggested that certain serine protease homologs (serine protease folds that lack an active catalytic triad) could be involved in the pathway. We generated a null mutant of the serine protease homolog spheroide (sphe). These mutant flies are susceptible to Enterococcus faecalis infection and unable to fully activate the Toll pathway. Sphe is required to activate the Toll pathway after challenge with pathogenic Gram-Positive bacteria. Sphe functions in the danger signal pathway, downstream or at the level of Persephone.},
keywords = {Fungi, Gram-Positive Bacteria, serine protease, spheroide, toll pathway},
pubstate = {published},
tppubtype = {article}
}
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}
}
Matskevich Alexey A, Quintin Jessica, Ferrandon Dominique
The Drosophila PRR GNBP3 assembles effector complexes involved in antifungal defenses independently of its Toll-pathway activation function Article de journal
Dans: Eur. J. Immunol., vol. 40, no. 5, p. 1244–1254, 2010, ISSN: 1521-4141.
Résumé | Liens | BibTeX | Étiquettes: Agglutination, Animals, Beauveria, Beauveria/immunology, Candida albicans, Candida albicans/immunology, Carrier Proteins, Carrier Proteins/*immunology/pharmacology, Drosophila melanogaster/*immunology/microbiology, Drosophila Proteins/*immunology/pharmacology/physiology, Enzyme Activation, ferrandon, Fungal, Fungi, Fungi/*immunology, Hemolymph, Hemolymph/immunology, M3i, Melanins, Melanins/*physiology, Monophenol Monooxygenase, Monophenol Monooxygenase/physiology, Multiprotein Complexes, Multiprotein Complexes/physiology, Recombinant Fusion Proteins, Recombinant Fusion Proteins/pharmacology, Serpins, Serpins/physiology, Spores, Toll-Like Receptors, Toll-Like Receptors/immunology
@article{matskevich_drosophila_2010b,
title = {The Drosophila PRR GNBP3 assembles effector complexes involved in antifungal defenses independently of its Toll-pathway activation function},
author = {Alexey A Matskevich and Jessica Quintin and Dominique Ferrandon},
doi = {10.1002/eji.200940164},
issn = {1521-4141},
year = {2010},
date = {2010-05-01},
journal = {Eur. J. Immunol.},
volume = {40},
number = {5},
pages = {1244--1254},
abstract = {The Drosophila Toll-signaling pathway controls the systemic antifungal host response. Gram-negative binding protein 3 (GNBP3), a member of the beta-glucan recognition protein family senses fungal infections and activates this pathway. A second detection system perceives the activity of proteolytic fungal virulence factors and redundantly activates Toll. GNBP3(hades) mutant flies succumb more rapidly to Candida albicans and to entomopathogenic fungal infections than WT flies, despite normal triggering of the Toll pathway via the virulence detection system. These observations suggest that GNBP3 triggers antifungal defenses that are not dependent on activation of the Toll pathway. Here, we show that GNBP3 agglutinates fungal cells. Furthermore, it can activate melanization in a Toll-independent manner. Melanization is likely to be an essential defense against some fungal infections given that the entomopathogenic fungus Beauveria bassiana inhibits the activity of the main melanization enzymes, the phenol oxidases. Finally, we show that GNBP3 assembles "attack complexes", which comprise phenoloxidase and the necrotic serpin. We propose that Drosophila GNBP3 targets fungi immediately at the inception of the infection by bringing effector molecules in direct contact with the invading microorganisms.},
keywords = {Agglutination, Animals, Beauveria, Beauveria/immunology, Candida albicans, Candida albicans/immunology, Carrier Proteins, Carrier Proteins/*immunology/pharmacology, Drosophila melanogaster/*immunology/microbiology, Drosophila Proteins/*immunology/pharmacology/physiology, Enzyme Activation, ferrandon, Fungal, Fungi, Fungi/*immunology, Hemolymph, Hemolymph/immunology, M3i, Melanins, Melanins/*physiology, Monophenol Monooxygenase, Monophenol Monooxygenase/physiology, Multiprotein Complexes, Multiprotein Complexes/physiology, Recombinant Fusion Proteins, Recombinant Fusion Proteins/pharmacology, Serpins, Serpins/physiology, Spores, Toll-Like Receptors, Toll-Like Receptors/immunology},
pubstate = {published},
tppubtype = {article}
}
Hetru Charles, Hoffmann Jules A
NF-kappaB in the immune response of Drosophila Article de journal
Dans: Cold Spring Harb Perspect Biol, vol. 1, no. 6, p. a000232, 2009, ISSN: 1943-0264.
Résumé | Liens | BibTeX | Étiquettes: Animals, bacteria, Fungi, Gene Expression Regulation, hoffmann, M3i, NF-kappa B
@article{hetru_nf-kappab_2009,
title = {NF-kappaB in the immune response of Drosophila},
author = {Charles Hetru and Jules A Hoffmann},
doi = {10.1101/cshperspect.a000232},
issn = {1943-0264},
year = {2009},
date = {2009-12-01},
journal = {Cold Spring Harb Perspect Biol},
volume = {1},
number = {6},
pages = {a000232},
abstract = {The nuclear factor kappaB (NF-kappaB) pathways play a major role in Drosophila host defense. Two recognition and signaling cascades control this immune response. The Toll pathway is activated by Gram-positive bacteria and by fungi, whereas the immune deficiency (Imd) pathway responds to Gram-negative bacterial infection. The basic mechanisms of recognition of these various types of microbial infections by the adult fly are now globally understood. Even though some elements are missing in the intracellular pathways, numerous proteins and interactions have been identified. In this article, we present a general picture of the immune functions of NF-kappaB in Drosophila with all the partners involved in recognition and in the signaling cascades.},
keywords = {Animals, bacteria, Fungi, Gene Expression Regulation, hoffmann, M3i, NF-kappa B},
pubstate = {published},
tppubtype = {article}
}
Chamy L El, Leclerc V, Caldelari I, Reichhart J-M
Sensing of 'danger signals' and pathogen-associated molecular patterns defines binary signaling pathways 'upstream' of Toll Article de journal
Dans: Nat. Immunol., vol. 9, no. 10, p. 1165–1170, 2008, ISSN: 1529-2916.
Résumé | Liens | BibTeX | Étiquettes: Animals, Fungi, Genetically Modified, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, In Situ Hybridization, M3i, Mycoses, Pattern Recognition, Peptide Hydrolases, Receptors, reichhart, ROMBY, Serine Endopeptidases, Signal Transduction, Toll-Like Receptors, Unité ARN
@article{el_chamy_sensing_2008,
title = {Sensing of 'danger signals' and pathogen-associated molecular patterns defines binary signaling pathways 'upstream' of Toll},
author = {L El Chamy and V Leclerc and I Caldelari and J-M Reichhart},
doi = {10.1038/ni.1643},
issn = {1529-2916},
year = {2008},
date = {2008-10-01},
journal = {Nat. Immunol.},
volume = {9},
number = {10},
pages = {1165--1170},
abstract = {In drosophila, molecular determinants from fungi and Gram-positive bacteria are detected by circulating pattern-recognition receptors. Published findings suggest that such pattern-recognition receptors activate as-yet-unidentified serine-protease cascades that culminate in the cleavage of Spätzle, the endogenous Toll receptor ligand, and trigger the immune response. We demonstrate here that the protease Grass defines a common activation cascade for the detection of fungi and Gram-positive bacteria mediated by pattern-recognition receptors. The serine protease Persephone, shown before to be specific for fungal detection in a cascade activated by secreted fungal proteases, was also required for the sensing of proteases elicited by bacteria in the hemolymph. Hence, Persephone defines a parallel proteolytic cascade activated by 'danger signals' such as abnormal proteolytic activities.},
keywords = {Animals, Fungi, Genetically Modified, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, In Situ Hybridization, M3i, Mycoses, Pattern Recognition, Peptide Hydrolases, Receptors, reichhart, ROMBY, Serine Endopeptidases, Signal Transduction, Toll-Like Receptors, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Wu Wei, Wieckowski Sébastien, Pastorin Giorgia, Benincasa Monica, Klumpp Cédric, Briand Jean-Paul, Gennaro Renato, Prato Maurizio, Bianco Alberto
Targeted delivery of amphotericin B to cells by using functionalized carbon nanotubes Article de journal
Dans: Angewandte Chemie (International Ed. in English), vol. 44, no. 39, p. 6358–6362, 2005, ISSN: 1433-7851.
Liens | BibTeX | Étiquettes: Amphotericin B, Antifungal Agents, carbon, Drug Carriers, Drug Delivery Systems, Fungi, Humans, I2CT, Jurkat Cells, Molecular Structure, Nanotubes, Particle Size, Solubility, Surface Properties, Team-Bianco
@article{wu_targeted_2005,
title = {Targeted delivery of amphotericin B to cells by using functionalized carbon nanotubes},
author = {Wei Wu and Sébastien Wieckowski and Giorgia Pastorin and Monica Benincasa and Cédric Klumpp and Jean-Paul Briand and Renato Gennaro and Maurizio Prato and Alberto Bianco},
doi = {10.1002/anie.200501613},
issn = {1433-7851},
year = {2005},
date = {2005-10-01},
journal = {Angewandte Chemie (International Ed. in English)},
volume = {44},
number = {39},
pages = {6358--6362},
keywords = {Amphotericin B, Antifungal Agents, carbon, Drug Carriers, Drug Delivery Systems, Fungi, Humans, I2CT, Jurkat Cells, Molecular Structure, Nanotubes, Particle Size, Solubility, Surface Properties, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Thouzeau Cécile, Maho Yvon Le, Froget Guillaume, Sabatier Laurence, Bohec Céline Le, Hoffmann Jules A, Bulet Philippe
Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus Article de journal
Dans: J. Biol. Chem., vol. 278, no. 51, p. 51053–51058, 2003, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry
@article{thouzeau_spheniscins_2003,
title = {Spheniscins, avian beta-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus},
author = {Cécile Thouzeau and Yvon Le Maho and Guillaume Froget and Laurence Sabatier and Céline Le Bohec and Jules A Hoffmann and Philippe Bulet},
doi = {10.1074/jbc.M306839200},
issn = {0021-9258},
year = {2003},
date = {2003-12-01},
journal = {J. Biol. Chem.},
volume = {278},
number = {51},
pages = {51053--51058},
abstract = {During the last part of egg incubation in king penguins, the male can preserve undigested food in the stomach for several weeks. This ensures survival of the newly hatched chick, in cases where the return of the foraging female from the sea is delayed. In accordance with the characterization of stress-induced bacteria, we demonstrate the occurrence of strong antimicrobial activities in preserved stomach contents. We isolated and fully characterized two isoforms of a novel 38-residue antimicrobial peptide (AMP), spheniscin, belonging to the beta-defensin subfamily. Spheniscin concentration was found to strongly increase during the period of food storage. Using a synthetic version of one of two spheniscin isoforms, we established that this peptide has a broad activity spectrum, affecting the growth of both pathogenic bacteria and fungi. Altogether, our data suggest that spheniscins and other, not yet identified, antimicrobial substances may play a role in the long term preservation of stored food in the stomach of king penguins.},
keywords = {Animals, Antimicrobial Cationic Peptides, bacteria, beta-Defensins, Birds, Feeding Behavior, Fungi, Gastrointestinal Contents, hoffmann, M3i, Male, Mass, Matrix-Assisted Laser Desorption-Ionization, Protein Isoforms, Sequence Alignment, Spectrometry},
pubstate = {published},
tppubtype = {article}
}
Bilak Hana, Tauszig-Delamasure S, Imler Jean-Luc
Toll and Toll-like receptors in Drosophila Article de journal
Dans: Biochemical Society Transactions, vol. 31, no. Pt 3, p. 648–651, 2003, ISSN: 0300-5127.
Résumé | Liens | BibTeX | Étiquettes: Animals, Biological Evolution, Cell Surface, Fungi, Genome, Gram-Negative Bacteria, Gram-Positive Bacteria, imler, M3i, Membrane Glycoproteins, Receptors, Toll-Like Receptor 5, Toll-Like Receptors
@article{bilak_toll_2003,
title = {Toll and Toll-like receptors in Drosophila},
author = {Hana Bilak and S Tauszig-Delamasure and Jean-Luc Imler},
doi = {10.1042/},
issn = {0300-5127},
year = {2003},
date = {2003-06-01},
journal = {Biochemical Society Transactions},
volume = {31},
number = {Pt 3},
pages = {648--651},
abstract = {The Drosophila Toll receptor controls the immune response to Gram-positive bacteria and fungi by activating a signalling pathway partially conserved throughout evolution. The Drosophila genome encodes eight additional Toll-related receptors, most of which appear to carry out developmental rather than immune functions. One exception may be Toll-9, which shares structural and functional similarities with mammalian TLRs.},
keywords = {Animals, Biological Evolution, Cell Surface, Fungi, Genome, Gram-Negative Bacteria, Gram-Positive Bacteria, imler, M3i, Membrane Glycoproteins, Receptors, Toll-Like Receptor 5, Toll-Like Receptors},
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}
}
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, 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}
}