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}
}
Shiao Shin-Hong, Whitten Miranda M A, Zachary Daniel, Hoffmann Jules A, Levashina Elena A
Fz2 and cdc42 mediate melanization and actin polymerization but are dispensable for Plasmodium killing in the mosquito midgut Article de journal
Dans: PLoS Pathog., vol. 2, no. 12, p. e133, 2006, ISSN: 1553-7374.
Résumé | Liens | BibTeX | Étiquettes: Actins, Animals, Anopheles, Carrier Proteins, cdc42 GTP-Binding Protein, Double-Stranded, Electron, Frizzled Receptors, Gastrointestinal Tract, hoffmann, Host-Parasite Interactions, Immunity, Innate, Insect Vectors, Intestinal Mucosa, M3i, Melanins, Microarray Analysis, Microscopy, Plasmodium berghei, Polymers, Protozoan, RNA, scanning, telomerase
@article{shiao_fz2_2006,
title = {Fz2 and cdc42 mediate melanization and actin polymerization but are dispensable for Plasmodium killing in the mosquito midgut},
author = {Shin-Hong Shiao and Miranda M A Whitten and Daniel Zachary and Jules A Hoffmann and Elena A Levashina},
doi = {10.1371/journal.ppat.0020133},
issn = {1553-7374},
year = {2006},
date = {2006-12-01},
journal = {PLoS Pathog.},
volume = {2},
number = {12},
pages = {e133},
abstract = {The midgut epithelium of the mosquito malaria vector Anopheles is a hostile environment for Plasmodium, with most parasites succumbing to host defenses. This study addresses morphological and ultrastructural features associated with Plasmodium berghei ookinete invasion in Anopheles gambiae midguts to define the sites and possible mechanisms of parasite killing. We show by transmission electron microscopy and immunofluorescence that the majority of ookinetes are killed in the extracellular space. Dead or dying ookinetes are surrounded by a polymerized actin zone formed within the basal cytoplasm of adjacent host epithelial cells. In refractory strain mosquitoes, we found that formation of this zone is strongly linked to prophenoloxidase activation leading to melanization. Furthermore, we identify two factors controlling both phenomena: the transmembrane receptor frizzled-2 and the guanosine triphosphate-binding protein cell division cycle 42. However, the disruption of actin polymerization and melanization by double-stranded RNA inhibition did not affect ookinete survival. Our results separate the mechanisms of parasite killing from subsequent reactions manifested by actin polymerization and prophenoloxidase activation in the A. gambiae-P. berghei model. These latter processes are reminiscent of wound healing in other organisms, and we propose that they represent a form of wound-healing response directed towards a moribund ookinete, which is perceived as damaged tissue.},
keywords = {Actins, Animals, Anopheles, Carrier Proteins, cdc42 GTP-Binding Protein, Double-Stranded, Electron, Frizzled Receptors, Gastrointestinal Tract, hoffmann, Host-Parasite Interactions, Immunity, Innate, Insect Vectors, Intestinal Mucosa, M3i, Melanins, Microarray Analysis, Microscopy, Plasmodium berghei, Polymers, Protozoan, RNA, scanning, telomerase},
pubstate = {published},
tppubtype = {article}
}
Ligoxygakis Petros, Pelte Nadège, Ji Chuanyi, Leclerc Vincent, Duvic Bernard, Belvin Marcia, Jiang Haobo, Hoffmann Jules A, Reichhart Jean-Marc
A serpin mutant links Toll activation to melanization in the host defence of Drosophila Article de journal
Dans: EMBO J., vol. 21, no. 23, p. 6330–6337, 2002, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Animals, Cell Surface, Hemolymph, hoffmann, infection, M3i, Melanins, Receptors, reichhart, Serpins, Toll-Like Receptors
@article{ligoxygakis_serpin_2002,
title = {A serpin mutant links Toll activation to melanization in the host defence of Drosophila},
author = {Petros Ligoxygakis and Nadège Pelte and Chuanyi Ji and Vincent Leclerc and Bernard Duvic and Marcia Belvin and Haobo Jiang and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {0261-4189},
year = {2002},
date = {2002-12-01},
journal = {EMBO J.},
volume = {21},
number = {23},
pages = {6330--6337},
abstract = {A prominent response during the Drosophila host defence is the induction of proteolytic cascades, some of which lead to localized melanization of pathogen surfaces, while others activate one of the major players in the systemic antimicrobial response, the Toll pathway. Despite the fact that gain-of-function mutations in the Toll receptor gene result in melanization, a clear link between Toll activation and the melanization reaction has not been firmly established. Here, we present evidence for the coordination of hemolymph-borne melanization with activation of the Toll pathway in the Drosophila host defence. The melanization reaction requires Toll pathway activation and depends on the removal of the Drosophila serine protease inhibitor Serpin27A. Flies deficient for this serpin exhibit spontaneous melanization in larvae and adults. Microbial challenge induces its removal from the hemolymph through Toll-dependent transcription of an acute phase immune reaction component.},
keywords = {Animals, Cell Surface, Hemolymph, hoffmann, infection, M3i, Melanins, Receptors, reichhart, Serpins, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Braun A, Hoffmann Jules A, Meister Marie
Analysis of the Drosophila host defense in domino mutant larvae, which are devoid of hemocytes Article de journal
Dans: Proc. Natl. Acad. Sci. U.S.A., vol. 95, no. 24, p. 14337–14342, 1998, ISSN: 0027-8424.
Résumé | BibTeX | Étiquettes: Adipose Tissue, Animals, Candida, Escherichia coli, Fungal, Genotype, Hemocytes, hoffmann, Larva, M3i, Melanins, Micrococcus luteus, Spores
@article{braun_analysis_1998,
title = {Analysis of the Drosophila host defense in domino mutant larvae, which are devoid of hemocytes},
author = {A Braun and Jules A Hoffmann and Marie Meister},
issn = {0027-8424},
year = {1998},
date = {1998-11-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {95},
number = {24},
pages = {14337--14342},
abstract = {We have analyzed the Drosophila immune response in domino mutant larvae, which are devoid of blood cells. The domino mutants have a good larval viability, but they die as prepupae. We show that, on immune challenge, induction of the genes encoding antimicrobial peptides in the fat body is not affected significantly in the mutant larvae, indicating that hemocytes are not essential in this process. The hemocoele of domino larvae contains numerous live microorganisms, the presence of which induces a weak antimicrobial response in the fat body. A full response is observed only after septic injury. We propose that the fat body cells are activated both by the presence of microorganisms and by injury and that injury potentiates the effect of microorganisms. Survival experiments after an immune challenge showed that domino mutants devoid of blood cells maintain a wild-type resistance to septic injury. This resistance was also observed in mutant larvae in which the synthesis of antibacterial peptides is impaired (immune deficiency larvae) and in mutants that are deficient for humoral melanization (Black cells larvae). However, if domino was combined with either the immune deficiency or the Black cell mutation, the resistance to septic injury was reduced severely. These results establish the relevance of the three immune reactions: phagocytosis, synthesis of antibacterial peptides, and melanization. By working in synergy, they provide Drosophila a highly effective defense against injury and/or infection.},
keywords = {Adipose Tissue, Animals, Candida, Escherichia coli, Fungal, Genotype, Hemocytes, hoffmann, Larva, M3i, Melanins, Micrococcus luteus, Spores},
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}
}