Publications
2021
Gasser Véronique, Kuhn Lauriane, Hubert Thibaut, Aussel Laurent, Hammann Philippe, Schalk Isabelle J.
The Esterase PfeE, the Achilles' Heel in the Battle for Iron between Pseudomonas aeruginosa and Escherichia coli Journal Article
In: International Journal of Molecular Sciences, vol. 22, no. 6, pp. 2814, 2021, ISSN: 1422-0067.
Abstract | Links | BibTeX | Tags: Carrier Proteins, co-cultures, enterobactin, Escherichia coli, Escherichia coli Proteins, Esterases, Iron, iron homeostasis, iron uptake, outer membrane transporters, PPSE, Pseudomonas aeruginosa, siderophore, TonB
@article{gasser_esterase_2021,
title = {The Esterase PfeE, the Achilles' Heel in the Battle for Iron between Pseudomonas aeruginosa and Escherichia coli},
author = {Véronique Gasser and Lauriane Kuhn and Thibaut Hubert and Laurent Aussel and Philippe Hammann and Isabelle J. Schalk},
doi = {10.3390/ijms22062814},
issn = {1422-0067},
year = {2021},
date = {2021-03-01},
urldate = {2021-03-01},
journal = {International Journal of Molecular Sciences},
volume = {22},
number = {6},
pages = {2814},
abstract = {Bacteria access iron, a key nutrient, by producing siderophores or using siderophores produced by other microorganisms. The pathogen Pseudomonas aeruginosa produces two siderophores but is also able to pirate enterobactin (ENT), the siderophore produced by Escherichia coli. ENT-Fe complexes are imported across the outer membrane of P. aeruginosa by the two outer membrane transporters PfeA and PirA. Iron is released from ENT in the P. aeruginosa periplasm by hydrolysis of ENT by the esterase PfeE. We show here that pfeE gene deletion renders P. aeruginosa unable to grow in the presence of ENT because it is unable to access iron via this siderophore. Two-species co-cultures under iron-restricted conditions show that P. aeruginosa strongly represses the growth of E. coli as long it is able to produce its own siderophores. Both strains are present in similar proportions in the culture as long as the siderophore-deficient P. aeruginosa strain is able to use ENT produced by E. coli to access iron. If pfeE is deleted, E. coli has the upper hand in the culture and P. aeruginosa growth is repressed. Overall, these data show that PfeE is the Achilles' heel of P. aeruginosa in communities with bacteria producing ENT.},
keywords = {Carrier Proteins, co-cultures, enterobactin, Escherichia coli, Escherichia coli Proteins, Esterases, Iron, iron homeostasis, iron uptake, outer membrane transporters, PPSE, Pseudomonas aeruginosa, siderophore, TonB},
pubstate = {published},
tppubtype = {article}
}
2013
Baron Olga Lucia, van West Pieter, Industri Benoit, Ponchet Michel, Dubreuil Géraldine, Gourbal Benjamin, Reichhart Jean-Marc, Coustau Christine
Parental transfer of the antimicrobial protein LBP/BPI protects Biomphalaria glabrata eggs against oomycete infections Journal Article
In: PLoS Pathog., vol. 9, no. 12, pp. e1003792, 2013, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: Acute-Phase Proteins, Animals, Antimicrobial Cationic Peptides, Biomphalaria, Blood Proteins, Carrier Proteins, Cell Membrane, Cell Membrane Permeability, Cloning, Escherichia coli, Female, Immunity, infection, M3i, Maternally-Acquired, Membrane Glycoproteins, Microbial Sensitivity Tests, Molecular, Oomycetes, Recombinant Proteins, reichhart, Zygote
@article{baron_parental_2013,
title = {Parental transfer of the antimicrobial protein LBP/BPI protects Biomphalaria glabrata eggs against oomycete infections},
author = {Olga Lucia Baron and Pieter van West and Benoit Industri and Michel Ponchet and Géraldine Dubreuil and Benjamin Gourbal and Jean-Marc Reichhart and Christine Coustau},
doi = {10.1371/journal.ppat.1003792},
issn = {1553-7374},
year = {2013},
date = {2013-01-01},
journal = {PLoS Pathog.},
volume = {9},
number = {12},
pages = {e1003792},
abstract = {Vertebrate females transfer antibodies via the placenta, colostrum and milk or via the egg yolk to protect their immunologically immature offspring against pathogens. This evolutionarily important transfer of immunity is poorly documented in invertebrates and basic questions remain regarding the nature and extent of parental protection of offspring. In this study, we show that a lipopolysaccharide binding protein/bactericidal permeability increasing protein family member from the invertebrate Biomphalaria glabrata (BgLBP/BPI1) is massively loaded into the eggs of this freshwater snail. Native and recombinant proteins displayed conserved LPS-binding, antibacterial and membrane permeabilizing activities. A broad screening of various pathogens revealed a previously unknown biocidal activity of the protein against pathogenic water molds (oomycetes), which is conserved in human BPI. RNAi-dependent silencing of LBP/BPI in the parent snails resulted in a significant reduction of reproductive success and extensive death of eggs through oomycete infections. This work provides the first functional evidence that a LBP/BPI is involved in the parental immune protection of invertebrate offspring and reveals a novel and conserved biocidal activity for LBP/BPI family members.},
keywords = {Acute-Phase Proteins, Animals, Antimicrobial Cationic Peptides, Biomphalaria, Blood Proteins, Carrier Proteins, Cell Membrane, Cell Membrane Permeability, Cloning, Escherichia coli, Female, Immunity, infection, M3i, Maternally-Acquired, Membrane Glycoproteins, Microbial Sensitivity Tests, Molecular, Oomycetes, Recombinant Proteins, reichhart, Zygote},
pubstate = {published},
tppubtype = {article}
}
2012
Schickel Jean-Nicolas, Pasquali Jean-Louis, Soley Anne, Knapp Anne-Marie, Decossas Marion, Kern Aurélie, Fauny Jean-Daniel, Marcellin Luc, Korganow Anne-Sophie, Martin Thierry, Soulas-Sprauel Pauline
Carabin deficiency in B cells increases BCR-TLR9 costimulation-induced autoimmunity Journal Article
In: EMBO molecular medicine, vol. 4, no. 12, pp. 1261–1275, 2012, ISSN: 1757-4684.
Abstract | Links | BibTeX | Tags: Adaptor Proteins, Animals, Antigen, Autoimmunity, B-Cell, B-Lymphocytes, Carrier Proteins, Cohort Studies, DNA, Humans, I2CT, Imagerie, Inbred NZB, Inbred Strains, Mice, Phosphorylation, Prospective Studies, Receptors, Signal Transducing, Toll-Like Receptor 9, Transfection
@article{schickel_carabin_2012,
title = {Carabin deficiency in B cells increases BCR-TLR9 costimulation-induced autoimmunity},
author = {Jean-Nicolas Schickel and Jean-Louis Pasquali and Anne Soley and Anne-Marie Knapp and Marion Decossas and Aurélie Kern and Jean-Daniel Fauny and Luc Marcellin and Anne-Sophie Korganow and Thierry Martin and Pauline Soulas-Sprauel},
doi = {10.1002/emmm.201201595},
issn = {1757-4684},
year = {2012},
date = {2012-01-01},
journal = {EMBO molecular medicine},
volume = {4},
number = {12},
pages = {1261--1275},
abstract = {The mechanisms behind flares of human autoimmune diseases in general, and of systemic lupus in particular, are poorly understood. The present scenario proposes that predisposing gene defects favour clinical flares under the influence of external stimuli. Here, we show that Carabin is low in B cells of (NZB × NZW) F1 mice (murine SLE model) long before the disease onset, and is low in B cells of lupus patients during the inactive phases of the disease. Using knock-out and B-cell-conditional knock-out murine models, we identify Carabin as a new negative regulator of B-cell function, whose deficiency in B cells speeds up early B-cell responses and makes the mice more susceptible to anti-dsDNA production and renal lupus flare after stimulation with a Toll-like Receptor 9 agonist, CpG-DNA. Finally, in vitro analysis of NFκB activation and Erk phosphorylation in TLR9- and B-cell receptor (BCR)-stimulated Carabin-deficient B cells strongly suggests how the internal defect synergizes with the external stimulus and proposes Carabin as a natural inhibitor of the potentially dangerous crosstalk between BCR and TLR9 pathways in self-reactive B cells.},
keywords = {Adaptor Proteins, Animals, Antigen, Autoimmunity, B-Cell, B-Lymphocytes, Carrier Proteins, Cohort Studies, DNA, Humans, I2CT, Imagerie, Inbred NZB, Inbred Strains, Mice, Phosphorylation, Prospective Studies, Receptors, Signal Transducing, Toll-Like Receptor 9, Transfection},
pubstate = {published},
tppubtype = {article}
}
2011
Nehme Nadine T, Quintin Jessica, Cho Ju Hyun, Lee Janice, Lafarge Marie-Céline, Kocks Christine, Ferrandon Dominique
Relative roles of the cellular and humoral responses in the Drosophila host defense against three gram-positive bacterial infections Journal Article
In: PLoS ONE, vol. 6, no. 3, pp. e14743, 2011, ISSN: 1932-6203.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Carrier Proteins, Cell Surface, Cellular, Enterococcus faecalis, ferrandon, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, Host-Pathogen Interactions, Humoral, Immunity, Innate, M3i, Micrococcus luteus, Opsonin Proteins, Phagocytosis, Receptors, Signal Transduction, Solubility, Staphylococcus aureus
@article{nehme_relative_2011b,
title = {Relative roles of the cellular and humoral responses in the Drosophila host defense against three gram-positive bacterial infections},
author = {Nadine T Nehme and Jessica Quintin and Ju Hyun Cho and Janice Lee and Marie-Céline Lafarge and Christine Kocks and Dominique Ferrandon},
doi = {10.1371/journal.pone.0014743},
issn = {1932-6203},
year = {2011},
date = {2011-01-01},
journal = {PLoS ONE},
volume = {6},
number = {3},
pages = {e14743},
abstract = {BACKGROUND: Two NF-kappaB signaling pathways, Toll and immune deficiency (imd), are required for survival to bacterial infections in Drosophila. In response to septic injury, these pathways mediate rapid transcriptional activation of distinct sets of effector molecules, including antimicrobial peptides, which are important components of a humoral defense response. However, it is less clear to what extent macrophage-like hemocytes contribute to host defense. METHODOLOGY/PRINCIPAL FINDINGS: In order to dissect the relative importance of humoral and cellular defenses after septic injury with three different gram-positive bacteria (Micrococcus luteus, Enterococcus faecalis, Staphylococcus aureus), we used latex bead pre-injection to ablate macrophage function in flies wildtype or mutant for various Toll and imd pathway components. We found that in all three infection models a compromised phagocytic system impaired fly survival--independently of concomitant Toll or imd pathway activation. Our data failed to confirm a role of the PGRP-SA and GNBP1 Pattern Recognition Receptors for phagocytosis of S. aureus. The Drosophila scavenger receptor Eater mediates the phagocytosis by hemocytes or S2 cells of E. faecalis and S. aureus, but not of M. luteus. In the case of M. luteus and E. faecalis, but not S. aureus, decreased survival due to defective phagocytosis could be compensated for by genetically enhancing the humoral immune response. CONCLUSIONS/SIGNIFICANCE: Our results underscore the fundamental importance of both cellular and humoral mechanisms in Drosophila immunity and shed light on the balance between these two arms of host defense depending on the invading pathogen.},
keywords = {Animals, Antimicrobial Cationic Peptides, Carrier Proteins, Cell Surface, Cellular, Enterococcus faecalis, ferrandon, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, Host-Pathogen Interactions, Humoral, Immunity, Innate, M3i, Micrococcus luteus, Opsonin Proteins, Phagocytosis, Receptors, Signal Transduction, Solubility, Staphylococcus aureus},
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}
}
2009
Mishima Yumiko, Quintin Jessica, Aimanianda Vishukumar, Kellenberger Christine, Coste Franck, Clavaud Cecile, Hetru Charles, Hoffmann Jules A, Latgé Jean-Paul, Ferrandon Dominique, Roussel Alain
The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors Journal Article
In: J. Biol. Chem., vol. 284, no. 42, pp. 28687–28697, 2009, ISSN: 1083-351X.
Abstract | Links | BibTeX | Tags: Animals, beta-Glucans, Bombyx, Carrier Proteins, Crystallography, ferrandon, Fungal Proteins, Hemolymph, hoffmann, ligands, M3i, Molecular Conformation, Mutagenesis, Polysaccharides, Protein Structure, Secondary, Tertiary, X-Ray
@article{mishima_n-terminal_2009,
title = {The N-terminal domain of Drosophila Gram-negative binding protein 3 (GNBP3) defines a novel family of fungal pattern recognition receptors},
author = {Yumiko Mishima and Jessica Quintin and Vishukumar Aimanianda and Christine Kellenberger and Franck Coste and Cecile Clavaud and Charles Hetru and Jules A Hoffmann and Jean-Paul Latgé and Dominique Ferrandon and Alain Roussel},
doi = {10.1074/jbc.M109.034587},
issn = {1083-351X},
year = {2009},
date = {2009-10-01},
journal = {J. Biol. Chem.},
volume = {284},
number = {42},
pages = {28687--28697},
abstract = {Gram-negative binding protein 3 (GNBP3), a pattern recognition receptor that circulates in the hemolymph of Drosophila, is responsible for sensing fungal infection and triggering Toll pathway activation. Here, we report that GNBP3 N-terminal domain binds to fungi upon identifying long chains of beta-1,3-glucans in the fungal cell wall as a major ligand. Interestingly, this domain fails to interact strongly with short oligosaccharides. The crystal structure of GNBP3-Nter reveals an immunoglobulin-like fold in which the glucan binding site is masked by a loop that is highly conserved among glucan-binding proteins identified in several insect orders. Structure-based mutagenesis experiments reveal an essential role for this occluding loop in discriminating between short and long polysaccharides. The displacement of the occluding loop is necessary for binding and could explain the specificity of the interaction with long chain structured polysaccharides. This represents a novel mechanism for beta-glucan recognition.},
keywords = {Animals, beta-Glucans, Bombyx, Carrier Proteins, Crystallography, ferrandon, Fungal Proteins, Hemolymph, hoffmann, ligands, M3i, Molecular Conformation, Mutagenesis, Polysaccharides, Protein Structure, Secondary, Tertiary, X-Ray},
pubstate = {published},
tppubtype = {article}
}
2006
Gottar Marie, Gobert Vanessa, Matskevich Alexey A, Reichhart Jean-Marc, Wang Chengshu, Butt Tariq M, Belvin Marcia, Hoffmann Jules A, Ferrandon Dominique
Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors Journal Article
In: Cell, vol. 127, no. 7, pp. 1425–1437, 2006, ISSN: 0092-8674.
Abstract | Links | BibTeX | Tags: Animals, Antibody Formation, Beauveria, Candida albicans, Carrier Proteins, Cellular, ferrandon, Glucans, hoffmann, Immunity, Immunological, M3i, Metarhizium, Models, Polysaccharides, reichhart, Serine Endopeptidases, Signal Transduction, Virulence Factors
@article{gottar_dual_2006,
title = {Dual detection of fungal infections in Drosophila via recognition of glucans and sensing of virulence factors},
author = {Marie Gottar and Vanessa Gobert and Alexey A Matskevich and Jean-Marc Reichhart and Chengshu Wang and Tariq M Butt and Marcia Belvin and Jules A Hoffmann and Dominique Ferrandon},
doi = {10.1016/j.cell.2006.10.046},
issn = {0092-8674},
year = {2006},
date = {2006-12-01},
journal = {Cell},
volume = {127},
number = {7},
pages = {1425--1437},
abstract = {The Drosophila immune system discriminates between various types of infections and activates appropriate signal transduction pathways to combat the invading microorganisms. The Toll pathway is required for the host response against fungal and most Gram-positive bacterial infections. The sensing of Gram-positive bacteria is mediated by the pattern recognition receptors PGRP-SA and GNBP1 that cooperate to detect the presence of infections in the host. Here, we report that GNBP3 is a pattern recognition receptor that is required for the detection of fungal cell wall components. Strikingly, we find that there is a second, parallel pathway acting jointly with GNBP3. The Drosophila Persephone protease activates the Toll pathway when proteolytically matured by the secreted fungal virulence factor PR1. Thus, the detection of fungal infections in Drosophila relies both on the recognition of invariant microbial patterns and on monitoring the effects of virulence factors on the host.},
keywords = {Animals, Antibody Formation, Beauveria, Candida albicans, Carrier Proteins, Cellular, ferrandon, Glucans, hoffmann, Immunity, Immunological, M3i, Metarhizium, Models, Polysaccharides, reichhart, Serine Endopeptidases, Signal Transduction, Virulence Factors},
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 Journal Article
In: PLoS Pathog., vol. 2, no. 12, pp. e133, 2006, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: 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}
}
Evans J D, Aronstein K, Chen Y P, Hetru Charles, Imler Jean-Luc, Jiang H, Kanost M, Thompson G J, Zou Z, Hultmark D
Immune pathways and defence mechanisms in honey bees Apis mellifera Journal Article
In: Insect Molecular Biology, vol. 15, no. 5, pp. 645–656, 2006, ISSN: 0962-1075.
Abstract | Links | BibTeX | Tags: Animals, Bees, Carrier Proteins, Genome, imler, Immunity, Insect, Janus Kinases, M3i, Multigene Family, Serine Endopeptidases, Signal Transduction, STAT Transcription Factors, Toll-Like Receptors
@article{evans_immune_2006,
title = {Immune pathways and defence mechanisms in honey bees Apis mellifera},
author = {J D Evans and K Aronstein and Y P Chen and Charles Hetru and Jean-Luc Imler and H Jiang and M Kanost and G J Thompson and Z Zou and D Hultmark},
doi = {10.1111/j.1365-2583.2006.00682.x},
issn = {0962-1075},
year = {2006},
date = {2006-10-01},
journal = {Insect Molecular Biology},
volume = {15},
number = {5},
pages = {645--656},
abstract = {Social insects are able to mount both group-level and individual defences against pathogens. Here we focus on individual defences, by presenting a genome-wide analysis of immunity in a social insect, the honey bee Apis mellifera. We present honey bee models for each of four signalling pathways associated with immunity, identifying plausible orthologues for nearly all predicted pathway members. When compared to the sequenced Drosophila and Anopheles genomes, honey bees possess roughly one-third as many genes in 17 gene families implicated in insect immunity. We suggest that an implied reduction in immune flexibility in bees reflects either the strength of social barriers to disease, or a tendency for bees to be attacked by a limited set of highly coevolved pathogens.},
keywords = {Animals, Bees, Carrier Proteins, Genome, imler, Immunity, Insect, Janus Kinases, M3i, Multigene Family, Serine Endopeptidases, Signal Transduction, STAT Transcription Factors, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Bischoff Vincent, Vignal Cécile, Duvic Bernard, Boneca Ivo G, Hoffmann Jules A, Royet Julien
Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2 Journal Article
In: PLoS Pathog., vol. 2, no. 2, pp. e14, 2006, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, bacteria, Carrier Proteins, Down-Regulation, hoffmann, Larva, M3i, RNA Interference, Signal Transduction
@article{bischoff_downregulation_2006,
title = {Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2},
author = {Vincent Bischoff and Cécile Vignal and Bernard Duvic and Ivo G Boneca and Jules A Hoffmann and Julien Royet},
doi = {10.1371/journal.ppat.0020014},
issn = {1553-7374},
year = {2006},
date = {2006-02-01},
journal = {PLoS Pathog.},
volume = {2},
number = {2},
pages = {e14},
abstract = {Peptidoglycan-recognition proteins (PGRPs) are evolutionarily conserved molecules that are structurally related to bacterial amidases. Several Drosophila PGRPs have lost this enzymatic activity and serve as microbe sensors through peptidoglycan recognition. Other PGRP family members, such as Drosophila PGRP-SC1 or mammalian PGRP-L, have conserved the amidase function and are able to cleave peptidoglycan in vitro. However, the contribution of these amidase PGRPs to host defense in vivo has remained elusive so far. Using an RNA-interference approach, we addressed the function of two PGRPs with amidase activity in the Drosophila immune response. We observed that PGRP-SC1/2-depleted flies present a specific over-activation of the IMD (immune deficiency) signaling pathway after bacterial challenge. Our data suggest that these proteins act in the larval gut to prevent activation of this pathway following bacterial ingestion. We further show that a strict control of IMD-pathway activation is essential to prevent bacteria-induced developmental defects and larval death.},
keywords = {Animals, Antimicrobial Cationic Peptides, bacteria, Carrier Proteins, Down-Regulation, hoffmann, Larva, M3i, RNA Interference, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Barbaroux Jean-Baptiste, Kwan Wing-Hong, Allam Jean-Pierre, Novak Natalija, Bieber Thomas, Fridman Wolf H, Groves Richard, Mueller Chris G
Tumor necrosis factor-alpha- and IL-4-independent development of Langerhans cell-like dendritic cells from M-CSF-conditioned precursors Journal Article
In: The Journal of Investigative Dermatology, vol. 126, no. 1, pp. 114–120, 2006, ISSN: 0022-202X.
Abstract | Links | BibTeX | Tags: Antigens, C-Type, Carrier Proteins, CC, CCR6, CD, CD1, CD34, Cell Differentiation, Chemokine, Chemokine CCL20, chemokines, Cytokines, DERMIS, FRANZ, Granulocyte-Macrophage Colony-Stimulating Factor, Hematopoietic Stem Cells, Humans, IL-4, Interleukin-4, Langerhans Cells, Lectins, Lipopolysaccharide Receptors, M-CSF, Macrophage Colony-Stimulating Factor, Macrophage Inflammatory Proteins, Mannose-Binding Lectins, Membrane Glycoproteins, murine, RANK ligand, Receptor Activator of Nuclear Factor-kappa B, Receptors, Surface, Team-Mueller, TNF ALPHA, Tumor Necrosis Factor-alpha
@article{barbaroux_tumor_2006,
title = {Tumor necrosis factor-alpha- and IL-4-independent development of Langerhans cell-like dendritic cells from M-CSF-conditioned precursors},
author = {Jean-Baptiste Barbaroux and Wing-Hong Kwan and Jean-Pierre Allam and Natalija Novak and Thomas Bieber and Wolf H Fridman and Richard Groves and Chris G Mueller},
doi = {10.1038/sj.jid.5700023},
issn = {0022-202X},
year = {2006},
date = {2006-01-01},
journal = {The Journal of Investigative Dermatology},
volume = {126},
number = {1},
pages = {114--120},
abstract = {GM-CSF and transforming growth factor beta (TGFbeta ) are required for the generation of Langerhans cells (LC), members of the dendritic cell (DC) family. Tumor necrosis factor alpha (TNFalpha) and IL-4 can enhance LC differentiation from human monocytes or CD34(+) progenitors. Here, we show that M-CSF-cultured DC precursors derived from CD34(+) progenitors resemble dermal CD14(+) cells and readily convert to LC-like DC in GM-CSF/TGFbeta. The cells express Langerin, CD1a, and CCR6, migrate in response to CCR6 ligand CCL20, and contain Birbeck granules. TNFalpha and IL-4, added separately or together, have an inhibitory effect on LC differentiation. Cells differentiated in the presence of IL-4 and TNFalpha express low levels of CCR7. This suggests that M-CSF-conditioned DC precursors retain the capacity to efficiently undergo a differentiation program, giving rise to LC-like DC solely through the effect of GM-CSF and TGFbeta.},
keywords = {Antigens, C-Type, Carrier Proteins, CC, CCR6, CD, CD1, CD34, Cell Differentiation, Chemokine, Chemokine CCL20, chemokines, Cytokines, DERMIS, FRANZ, Granulocyte-Macrophage Colony-Stimulating Factor, Hematopoietic Stem Cells, Humans, IL-4, Interleukin-4, Langerhans Cells, Lectins, Lipopolysaccharide Receptors, M-CSF, Macrophage Colony-Stimulating Factor, Macrophage Inflammatory Proteins, Mannose-Binding Lectins, Membrane Glycoproteins, murine, RANK ligand, Receptor Activator of Nuclear Factor-kappa B, Receptors, Surface, Team-Mueller, TNF ALPHA, Tumor Necrosis Factor-alpha},
pubstate = {published},
tppubtype = {article}
}
2004
Bischoff Vincent, Vignal Cécile, Boneca Ivo G, Michel Tatiana, Hoffmann Jules A, Royet Julien
Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria Journal Article
In: Nat. Immunol., vol. 5, no. 11, pp. 1175–1180, 2004, ISSN: 1529-2908.
Abstract | Links | BibTeX | Tags: Animals, Carrier Proteins, Cell Surface, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, hoffmann, M3i, Mutation, Mycoses, Receptors, Staphylococcus aureus, Toll-Like Receptors
@article{bischoff_function_2004,
title = {Function of the drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria},
author = {Vincent Bischoff and Cécile Vignal and Ivo G Boneca and Tatiana Michel and Jules A Hoffmann and Julien Royet},
doi = {10.1038/ni1123},
issn = {1529-2908},
year = {2004},
date = {2004-11-01},
journal = {Nat. Immunol.},
volume = {5},
number = {11},
pages = {1175--1180},
abstract = {The activation of an immune response requires recognition of microorganisms by host receptors. In drosophila, detection of Gram-positive bacteria is mediated by cooperation between the peptidoglycan-recognition protein-SA (PGRP-SA) and Gram-negative binding protein 1 (GNBP1) proteins. Here we show that some Gram-positive bacterial species activate an immune response in a PGRP-SA- and GNBP1-independent manner, indicating that alternative receptors exist. Consistent with this, we noted that PGRP-SD mutants were susceptible to some Gram-positive bacteria and that a loss-of-function mutation in PGRP-SD severely exacerbated the PGRP-SA and GNBP1 mutant phenotypes. These data indicate that PGRP-SD can function as a receptor for Gram-positive bacteria and shows partial redundancy with the PGRP-SA-GNBP1 complex.},
keywords = {Animals, Carrier Proteins, Cell Surface, Gram-Positive Bacteria, Gram-Positive Bacterial Infections, hoffmann, M3i, Mutation, Mycoses, Receptors, Staphylococcus aureus, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
2003
Royet Julien, Reichhart Jean-Marc
Detection of peptidoglycans by NOD proteins Journal Article
In: Trends Cell Biol., vol. 13, no. 12, pp. 610–614, 2003, ISSN: 0962-8924.
Abstract | BibTeX | Tags: Adaptor Proteins, Apoptosis, Carrier Proteins, Gram-Positive Bacteria, Humans, Immunity, Immunologic, Innate, M3i, Nod1 Signaling Adaptor Protein, Oligopeptides, peptidoglycan, Receptors, reichhart, Signal Transducing, Signal Transduction
@article{royet_detection_2003,
title = {Detection of peptidoglycans by NOD proteins},
author = {Julien Royet and Jean-Marc Reichhart},
issn = {0962-8924},
year = {2003},
date = {2003-12-01},
journal = {Trends Cell Biol.},
volume = {13},
number = {12},
pages = {610--614},
abstract = {Mechanisms of innate immune defense are based on the recognition of invariant microbial molecular patterns by specific receptors, followed by the activation of signaling pathways and the expression of effector molecules that will defeat the invading microorganism. Two recent reports add to the growing list of these pattern-recognition receptors by showing that the intracellular nucleotide-binding oligomerization domain 1 (NOD1) protein recognizes a diaminopimelate-containing muropeptide, a cell-wall component of Gram-negative bacteria.},
keywords = {Adaptor Proteins, Apoptosis, Carrier Proteins, Gram-Positive Bacteria, Humans, Immunity, Immunologic, Innate, M3i, Nod1 Signaling Adaptor Protein, Oligopeptides, peptidoglycan, Receptors, reichhart, Signal Transducing, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
Gobert Vanessa, Gottar Marie, Matskevich Alexey A, Rutschmann Sophie, Royet Julien, Belvin Marcia, Hoffmann Jules A, Ferrandon Dominique
Dual activation of the Drosophila toll pathway by two pattern recognition receptors Journal Article
In: Science, vol. 302, no. 5653, pp. 2126–2130, 2003, ISSN: 1095-9203.
Abstract | Links | BibTeX | Tags: Animals, Carrier Proteins, Cell Surface, DNA Transposable Elements, ferrandon, Gene Expression, Genes, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolymph, hoffmann, Hypocreales, Insect, Insect Proteins, M3i, Mutation, Phenotype, Receptors, Serine Endopeptidases, Toll-Like Receptors
@article{gobert_dual_2003,
title = {Dual activation of the Drosophila toll pathway by two pattern recognition receptors},
author = {Vanessa Gobert and Marie Gottar and Alexey A Matskevich and Sophie Rutschmann and Julien Royet and Marcia Belvin and Jules A Hoffmann and Dominique Ferrandon},
doi = {10.1126/science.1085432},
issn = {1095-9203},
year = {2003},
date = {2003-12-01},
journal = {Science},
volume = {302},
number = {5653},
pages = {2126--2130},
abstract = {The Toll-dependent defense against Gram-positive bacterial infections in Drosophila is mediated through the peptidoglycan recognition protein SA (PGRP-SA). A mutation termed osiris disrupts the Gram-negative binding protein 1 (GNBP1) gene and leads to compromised survival of mutant flies after Gram-positive infections, but not after fungal or Gram-negative bacterial challenge. Our results demonstrate that GNBP1 and PGRP-SA can jointly activate the Toll pathway. The potential for a combination of distinct proteins to mediate detection of infectious nonself in the fly will refine the concept of pattern recognition in insects.},
keywords = {Animals, Carrier Proteins, Cell Surface, DNA Transposable Elements, ferrandon, Gene Expression, Genes, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolymph, hoffmann, Hypocreales, Insect, Insect Proteins, M3i, Mutation, Phenotype, Receptors, Serine Endopeptidases, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
2002
Naitza Silvia, Rossé Carine, Kappler Christine, Georgel Philippe, Belvin Marcia, Gubb David, Camonis Jacques, Hoffmann Jules A, Reichhart Jean-Marc
The Drosophila immune defense against gram-negative infection requires the death protein dFADD Journal Article
In: Immunity, vol. 17, no. 5, pp. 575–581, 2002, ISSN: 1074-7613.
Abstract | BibTeX | Tags: Adaptor Proteins, Animals, Carrier Proteins, Fas-Associated Death Domain Protein, Gene Expression Regulation, Gram-Negative Bacterial Infections, hoffmann, Immunity, M3i, reichhart, Signal Transducing, Signal Transduction
@article{naitza_drosophila_2002,
title = {The Drosophila immune defense against gram-negative infection requires the death protein dFADD},
author = {Silvia Naitza and Carine Rossé and Christine Kappler and Philippe Georgel and Marcia Belvin and David Gubb and Jacques Camonis and Jules A Hoffmann and Jean-Marc Reichhart},
issn = {1074-7613},
year = {2002},
date = {2002-11-01},
journal = {Immunity},
volume = {17},
number = {5},
pages = {575--581},
abstract = {Drosophila responds to Gram-negative infections by mounting an immune response that depends on components of the IMD pathway. We recently showed that imd encodes a protein with a death domain with high similarity to that of mammalian RIP. Using a two-hybrid screen in yeast, we have isolated the death protein dFADD as a molecule that associates with IMD. Our data show that loss of dFADD function renders flies highly susceptible to Gram-negative infections without affecting resistance to Gram-positive bacteria. By genetic analysis we show that dFADD acts downstream of IMD in the pathway that controls inducibility of the antibacterial peptide genes.},
keywords = {Adaptor Proteins, Animals, Carrier Proteins, Fas-Associated Death Domain Protein, Gene Expression Regulation, Gram-Negative Bacterial Infections, hoffmann, Immunity, M3i, reichhart, Signal Transducing, Signal Transduction},
pubstate = {published},
tppubtype = {article}
}
2001
Michel T, Reichhart Jean-Marc, Hoffmann Jules A, Royet Julien
Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein Journal Article
In: Nature, vol. 414, no. 6865, pp. 756–759, 2001, ISSN: 0028-0836.
Abstract | Links | BibTeX | Tags: 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}
}
1975
Feyereisen R, Lagueux Marie, Hoffmann Jules A
The hemolymphatic transport of molting hormone during the development of Locusta migratoria L Journal Article
In: C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat., vol. 280, no. 14, pp. 1709–1712, 1975.
Abstract | BibTeX | Tags: Age Factors, Animals, Carrier Proteins, Chromatography, Ecdysone, Ecdysterone, Gel, Grasshoppers, Hematopoietic System, hoffmann, Larva, M3i, Neurosecretory Systems, Protein Binding, Time Factors
@article{feyereisen_hemolymphatic_1975,
title = {The hemolymphatic transport of molting hormone during the development of Locusta migratoria L},
author = {R Feyereisen and Marie Lagueux and Jules A Hoffmann},
year = {1975},
date = {1975-04-01},
journal = {C.R. Hebd. Seances Acad. Sci., Ser. D, Sci. Nat.},
volume = {280},
number = {14},
pages = {1709--1712},
abstract = {Shortly after injection of radio-labelled ecdysone into fifth instar larvae of Locusta migratoria, 20-hydroxy-ecdysone (ecdysterone) is the main hormone found in the blood. Some 10% of the circulating hormone are bound to hemolymph macromolecules. The ratio of bound to free hormone is stage-dependent; it decreases considerably after previous injections of non-labelled ecdysone, but increases in insects in which ecdysone biosynthesis has been blocked by extirpation of the prothoracic glands or selective X-ray treatment of the hemocytopoietic tissue.},
keywords = {Age Factors, Animals, Carrier Proteins, Chromatography, Ecdysone, Ecdysterone, Gel, Grasshoppers, Hematopoietic System, hoffmann, Larva, M3i, Neurosecretory Systems, Protein Binding, Time Factors},
pubstate = {published},
tppubtype = {article}
}