Publications
2011
Boyer Laurent, Magoc Lorin, Dejardin Stephanie, Cappillino Michael, Paquette Nicholas, Hinault Charlotte, Charriere Guillaume M, Ip Eddie W K, Fracchia Shannon, Hennessy Elizabeth, Erturk-Hasdemir Deniz, Reichhart Jean-Marc, Silverman Neal, Lacy-Hulbert Adam, Stuart Lynda M
Pathogen-derived effectors trigger protective immunity via activation of the Rac2 enzyme and the IMD or Rip kinase signaling pathway Journal Article
In: Immunity, vol. 35, no. 4, pp. 536–549, 2011, ISSN: 1097-4180.
Abstract | Links | BibTeX | Tags: Adaptor Proteins, Enzyme Activation, HEK293 Cells, Humans, M3i, rac GTP-Binding Proteins, Receptor-Interacting Protein Serine-Threonine Kinases, reichhart, Signal Transducing, Signal Transduction
@article{boyer_pathogen-derived_2011,
title = {Pathogen-derived effectors trigger protective immunity via activation of the Rac2 enzyme and the IMD or Rip kinase signaling pathway},
author = {Laurent Boyer and Lorin Magoc and Stephanie Dejardin and Michael Cappillino and Nicholas Paquette and Charlotte Hinault and Guillaume M Charriere and Eddie W K Ip and Shannon Fracchia and Elizabeth Hennessy and Deniz Erturk-Hasdemir and Jean-Marc Reichhart and Neal Silverman and Adam Lacy-Hulbert and Lynda M Stuart},
doi = {10.1016/j.immuni.2011.08.015},
issn = {1097-4180},
year = {2011},
date = {2011-10-01},
journal = {Immunity},
volume = {35},
number = {4},
pages = {536--549},
abstract = {Although infections with virulent pathogens often induce a strong inflammatory reaction, what drives the increased immune response to pathogens compared to nonpathogenic microbes is poorly understood. One possibility is that the immune system senses the level of threat from a microorganism and augments the response accordingly. Here, focusing on cytotoxic necrotizing factor 1 (CNF1), an Escherichia coli-derived effector molecule, we showed the host indirectly sensed the pathogen by monitoring for the effector that modified RhoGTPases. CNF1 modified Rac2, which then interacted with the innate immune adaptors IMD and Rip1-Rip2 in flies and mammalian cells, respectively, to drive an immune response. This response was protective and increased the ability of the host to restrict pathogen growth, thus defining a mechanism of effector-triggered immunity that contributes to how metazoans defend against microbes with pathogenic potential.},
keywords = {Adaptor Proteins, Enzyme Activation, HEK293 Cells, Humans, M3i, rac GTP-Binding Proteins, Receptor-Interacting Protein Serine-Threonine Kinases, reichhart, Signal Transducing, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
2010
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 Journal Article
In: Eur. J. Immunol., vol. 40, no. 5, pp. 1244–1254, 2010, ISSN: 1521-4141.
Abstract | Links | BibTeX | Tags: 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}
}
2006
Leclerc Vincent, Pelte Nadège, Chamy Laure El, Martinelli Cosimo, Ligoxygakis Petros, Hoffmann Jules A, Reichhart Jean-Marc
Prophenoloxidase activation is not required for survival to microbial infections in Drosophila Journal Article
In: EMBO Rep., vol. 7, no. 2, pp. 231–235, 2006, ISSN: 1469-221X.
Abstract | Links | BibTeX | Tags: Animals, Bacterial Infections, Catechol Oxidase, Enzyme Activation, Enzyme Precursors, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolymph, hoffmann, Immunity, Innate, M3i, Mutation, reichhart, Survival Rate
@article{leclerc_prophenoloxidase_2006,
title = {Prophenoloxidase activation is not required for survival to microbial infections in Drosophila},
author = {Vincent Leclerc and Nadège Pelte and Laure El Chamy and Cosimo Martinelli and Petros Ligoxygakis and Jules A Hoffmann and Jean-Marc Reichhart},
doi = {10.1038/sj.embor.7400592},
issn = {1469-221X},
year = {2006},
date = {2006-02-01},
journal = {EMBO Rep.},
volume = {7},
number = {2},
pages = {231--235},
abstract = {The antimicrobial defence of Drosophila relies on cellular and humoral processes, of which the inducible synthesis of antimicrobial peptides has attracted interest in recent years. Another potential line of defence is the activation, by a proteolytic cascade, of phenoloxidase, which leads to the production of quinones and melanin. However, in spite of several publications on this subject, the contribution of phenoloxidase activation to resistance to infections has not been established under appropriate in vivo conditions. Here, we have isolated the first Drosophila mutant for a prophenoloxidase-activating enzyme (PAE1). In contrast to wild-type flies, PAE1 mutants fail to activate phenoloxidase in the haemolymph following microbial challenge. Surprisingly, we find that these mutants are as resistant to infections as wild-type flies, in the total absence of circulating phenoloxidase activity. This raises the question with regard to the precise function of phenoloxidase activation in defence, if any.},
keywords = {Animals, Bacterial Infections, Catechol Oxidase, Enzyme Activation, Enzyme Precursors, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolymph, hoffmann, Immunity, Innate, M3i, Mutation, reichhart, Survival Rate},
pubstate = {published},
tppubtype = {article}
}