Publications
2011 |
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Articles de journaux |
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| 14. | Imler, Jean-Luc; Ferrandon, Dominique [Innate immunity crowned 2011 Nobel Prize winner] Article de journal Med Sci (Paris), 27 , p. 1019–24, 2011, ISSN: 0767-0974 (Print) 0767-0974 (Linking). Liens | BibTeX | Étiquettes: *Immunity, *Nobel Prize, Biological, Genetic Association Studies, Humans, Immunotherapy/methods/trends, Innate/genetics, Models, Molecular Targeted Therapy/trends, Seasons, Structure-Activity Relationship, Toll-Like Receptors/chemistry/genetics/isolation & purification/physiology @article{imler_[innate_2011b, title = {[Innate immunity crowned 2011 Nobel Prize winner]}, author = {Jean-Luc Imler and Dominique Ferrandon}, url = {http://dx.doi.org.gate1.inist.fr/10.1051/medsci/20112711020}, doi = {10.1051/medsci/20112711020}, issn = {0767-0974 (Print) 0767-0974 (Linking)}, year = {2011}, date = {2011-11-01}, journal = {Med Sci (Paris)}, volume = {27}, pages = {1019--24}, keywords = {*Immunity, *Nobel Prize, Biological, Genetic Association Studies, Humans, Immunotherapy/methods/trends, Innate/genetics, Models, Molecular Targeted Therapy/trends, Seasons, Structure-Activity Relationship, Toll-Like Receptors/chemistry/genetics/isolation & purification/physiology}, pubstate = {published}, tppubtype = {article} } |
| 13. | Ogawa, Michinaga; Yoshikawa, Yuko; Kobayashi, Taira; Mimuro, Hitomi; Fukumatsu, Makoto; Kiga, Kotaro; Piao, Zhenzi; Ashida, Hiroshi; Yoshida, Mitsutaka; Kakuta, Shigeru; Koyama, Tomohiro; Goto, Yoshiyuki; Nagatake, Takahiro; Nagai, Shinya; Kiyono, Hiroshi; Kawalec, Magdalena; Reichhart, Jean-Marc; Sasakawa, Chihiro A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens Article de journal Cell Host Microbe, 9 (5), p. 376–389, 2011, ISSN: 1934-6069. Résumé | Liens | BibTeX | Étiquettes: Autophagy, Biological, Cells, Cultured, Membrane Proteins, Mice, Microtubule-Associated Proteins, Models, Phagosomes, Protein Interaction Mapping, Shigella, Two-Hybrid System Techniques @article{ogawa_tecpr1-dependent_2011, title = {A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens}, author = { Michinaga Ogawa and Yuko Yoshikawa and Taira Kobayashi and Hitomi Mimuro and Makoto Fukumatsu and Kotaro Kiga and Zhenzi Piao and Hiroshi Ashida and Mitsutaka Yoshida and Shigeru Kakuta and Tomohiro Koyama and Yoshiyuki Goto and Takahiro Nagatake and Shinya Nagai and Hiroshi Kiyono and Magdalena Kawalec and Jean-Marc Reichhart and Chihiro Sasakawa}, doi = {10.1016/j.chom.2011.04.010}, issn = {1934-6069}, year = {2011}, date = {2011-05-01}, journal = {Cell Host Microbe}, volume = {9}, number = {5}, pages = {376--389}, abstract = {Selective autophagy of bacterial pathogens represents a host innate immune mechanism. Selective autophagy has been characterized on the basis of distinct cargo receptors but the mechanisms by which different cargo receptors are targeted for autophagic degradation remain unclear. In this study we identified a highly conserved Tectonin domain-containing protein, Tecpr1, as an Atg5 binding partner that colocalized with Atg5 at Shigella-containing phagophores. Tecpr1 activity is necessary for efficient autophagic targeting of bacteria, but has no effect on rapamycin- or starvation-induced canonical autophagy. Tecpr1 interacts with WIPI-2, a yeast Atg18 homolog and PI(3)P-interacting protein required for phagophore formation, and they colocalize to phagophores. Although Tecpr1-deficient mice appear normal, Tecpr1-deficient MEFs were defective for selective autophagy and supported increased intracellular multiplication of Shigella. Further, depolarized mitochondria and misfolded protein aggregates accumulated in the Tecpr1-knockout MEFs. Thus, we identify a Tecpr1-dependent pathway as important in targeting bacterial pathogens for selective autophagy.}, keywords = {Autophagy, Biological, Cells, Cultured, Membrane Proteins, Mice, Microtubule-Associated Proteins, Models, Phagosomes, Protein Interaction Mapping, Shigella, Two-Hybrid System Techniques}, pubstate = {published}, tppubtype = {article} } Selective autophagy of bacterial pathogens represents a host innate immune mechanism. Selective autophagy has been characterized on the basis of distinct cargo receptors but the mechanisms by which different cargo receptors are targeted for autophagic degradation remain unclear. In this study we identified a highly conserved Tectonin domain-containing protein, Tecpr1, as an Atg5 binding partner that colocalized with Atg5 at Shigella-containing phagophores. Tecpr1 activity is necessary for efficient autophagic targeting of bacteria, but has no effect on rapamycin- or starvation-induced canonical autophagy. Tecpr1 interacts with WIPI-2, a yeast Atg18 homolog and PI(3)P-interacting protein required for phagophore formation, and they colocalize to phagophores. Although Tecpr1-deficient mice appear normal, Tecpr1-deficient MEFs were defective for selective autophagy and supported increased intracellular multiplication of Shigella. Further, depolarized mitochondria and misfolded protein aggregates accumulated in the Tecpr1-knockout MEFs. Thus, we identify a Tecpr1-dependent pathway as important in targeting bacterial pathogens for selective autophagy. |
| 12. | Lee, Kwang-Zin; Ferrandon, Dominique Negative regulation of immune responses on the fly Article de journal EMBO J., 30 (6), p. 988–990, 2011, ISSN: 1460-2075. Liens | BibTeX | Étiquettes: *Gene Expression Regulation, *Homeostasis, Bacteria, Bacteria/*immunology, Biological, Drosophila melanogaster/*immunology, Drosophila Proteins/biosynthesis/metabolism, Gene Expression Regulation, Homeostasis, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinases/metabolism, Models, NF-kappa B, NF-kappa B/metabolism, ras Proteins, ras Proteins/metabolism, Receptor Protein-Tyrosine Kinases, Receptor Protein-Tyrosine Kinases/metabolism @article{lee_negative_2011b, title = {Negative regulation of immune responses on the fly}, author = { Kwang-Zin Lee and Dominique Ferrandon}, doi = {10.1038/emboj.2011.47}, issn = {1460-2075}, year = {2011}, date = {2011-01-01}, journal = {EMBO J.}, volume = {30}, number = {6}, pages = {988--990}, keywords = {*Gene Expression Regulation, *Homeostasis, Bacteria, Bacteria/*immunology, Biological, Drosophila melanogaster/*immunology, Drosophila Proteins/biosynthesis/metabolism, Gene Expression Regulation, Homeostasis, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinases/metabolism, Models, NF-kappa B, NF-kappa B/metabolism, ras Proteins, ras Proteins/metabolism, Receptor Protein-Tyrosine Kinases, Receptor Protein-Tyrosine Kinases/metabolism}, pubstate = {published}, tppubtype = {article} } |
2010 |
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Articles de journaux |
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| 11. | Silverman, Gary A; Whisstock, James C; Bottomley, Stephen P; Huntington, James A; Kaiserman, Dion; Luke, Cliff J; Pak, Stephen C; Reichhart, Jean-Marc; Bird, Phillip I Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems Article de journal J. Biol. Chem., 285 (32), p. 24299–24305, 2010, ISSN: 1083-351X. Résumé | Liens | BibTeX | Étiquettes: Biological, Caenorhabditis elegans, Cell Death, Cell Differentiation, Cell Survival, Homeostasis, Humans, Immunity, Innate, Mice, Models, Phenotype, Serpins, Transgenes, Transgenic @article{silverman_serpins_2010, title = {Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems}, author = { Gary A. Silverman and James C. Whisstock and Stephen P. Bottomley and James A. Huntington and Dion Kaiserman and Cliff J. Luke and Stephen C. Pak and Jean-Marc Reichhart and Phillip I. Bird}, doi = {10.1074/jbc.R110.112771}, issn = {1083-351X}, year = {2010}, date = {2010-08-01}, journal = {J. Biol. Chem.}, volume = {285}, number = {32}, pages = {24299--24305}, abstract = {Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.}, keywords = {Biological, Caenorhabditis elegans, Cell Death, Cell Differentiation, Cell Survival, Homeostasis, Humans, Immunity, Innate, Mice, Models, Phenotype, Serpins, Transgenes, Transgenic}, pubstate = {published}, tppubtype = {article} } Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors. |
| 10. | Whisstock, James C; Silverman, Gary A; Bird, Phillip I; Bottomley, Stephen P; Kaiserman, Dion; Luke, Cliff J; Pak, Stephen C; Reichhart, Jean-Marc; Huntington, James A Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions Article de journal J. Biol. Chem., 285 (32), p. 24307–24312, 2010, ISSN: 1083-351X. Résumé | Liens | BibTeX | Étiquettes: Biological, Biological Transport, Biophysics, Catalytic Domain, Hormones, Humans, Kinetics, Models, Peptide Hydrolases, Protein Binding, Protein Conformation, Protein Structure, Serpins, Substrate Specificity, Tertiary, Thrombin @article{whisstock_serpins_2010, title = {Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions}, author = { James C. Whisstock and Gary A. Silverman and Phillip I. Bird and Stephen P. Bottomley and Dion Kaiserman and Cliff J. Luke and Stephen C. Pak and Jean-Marc Reichhart and James A. Huntington}, doi = {10.1074/jbc.R110.141408}, issn = {1083-351X}, year = {2010}, date = {2010-08-01}, journal = {J. Biol. Chem.}, volume = {285}, number = {32}, pages = {24307--24312}, abstract = {Inhibitory serpins are metastable proteins that undergo a substantial conformational rearrangement to covalently trap target peptidases. The serpin reactive center loop contributes a majority of the interactions that serpins make during the initial binding to target peptidases. However, structural studies on serpin-peptidase complexes reveal a broader set of contacts on the scaffold of inhibitory serpins that have substantial influence on guiding peptidase recognition. Structural and biophysical studies also reveal how aberrant serpin folding can lead to the formation of domain-swapped serpin multimers rather than the monomeric metastable state. Serpin domain swapping may therefore underlie the polymerization events characteristic of the serpinopathies. Finally, recent structural studies reveal how the serpin fold has been adapted for non-inhibitory functions such as hormone binding.}, keywords = {Biological, Biological Transport, Biophysics, Catalytic Domain, Hormones, Humans, Kinetics, Models, Peptide Hydrolases, Protein Binding, Protein Conformation, Protein Structure, Serpins, Substrate Specificity, Tertiary, Thrombin}, pubstate = {published}, tppubtype = {article} } Inhibitory serpins are metastable proteins that undergo a substantial conformational rearrangement to covalently trap target peptidases. The serpin reactive center loop contributes a majority of the interactions that serpins make during the initial binding to target peptidases. However, structural studies on serpin-peptidase complexes reveal a broader set of contacts on the scaffold of inhibitory serpins that have substantial influence on guiding peptidase recognition. Structural and biophysical studies also reveal how aberrant serpin folding can lead to the formation of domain-swapped serpin multimers rather than the monomeric metastable state. Serpin domain swapping may therefore underlie the polymerization events characteristic of the serpinopathies. Finally, recent structural studies reveal how the serpin fold has been adapted for non-inhibitory functions such as hormone binding. |
| 9. | Paquette, Nicholas; Broemer, Meike; Aggarwal, Kamna; Chen, Li; Husson, Marie; Ertürk-Hasdemir, Deniz; Reichhart, Jean-Marc; Meier, Pascal; Silverman, Neal Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-kappaB signaling Article de journal Mol. Cell, 37 (2), p. 172–182, 2010, ISSN: 1097-4164. Résumé | Liens | BibTeX | Étiquettes: Alleles, Amino Acid Motifs, Biological, Caspases, Inhibitor of Apoptosis Proteins, MAP Kinase Kinase Kinases, Models, NF-kappa B, Sequence Alignment, Signal Transduction, Ubiquitin-Protein Ligases, Ubiquitination @article{paquette_caspase-mediated_2010, title = {Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-kappaB signaling}, author = { Nicholas Paquette and Meike Broemer and Kamna Aggarwal and Li Chen and Marie Husson and Deniz Ertürk-Hasdemir and Jean-Marc Reichhart and Pascal Meier and Neal Silverman}, doi = {10.1016/j.molcel.2009.12.036}, issn = {1097-4164}, year = {2010}, date = {2010-01-01}, journal = {Mol. Cell}, volume = {37}, number = {2}, pages = {172--182}, abstract = {Innate immune responses are critical for the immediate protection against microbial infection. In Drosophila, infection leads to the rapid and robust production of antimicrobial peptides through two NF-kappaB signaling pathways-IMD and Toll. The IMD pathway is triggered by DAP-type peptidoglycan, common to most Gram-negative bacteria. Signaling downstream from the peptidoglycan receptors is thought to involve K63 ubiquitination and caspase-mediated cleavage, but the molecular mechanisms remain obscure. We now show that PGN stimulation causes caspase-mediated cleavage of the imd protein, exposing a highly conserved IAP-binding motif (IBM) at its neo-N terminus. A functional IBM is required for the association of cleaved IMD with the ubiquitin E3-ligase DIAP2. Through its association with DIAP2, IMD is rapidly conjugated with K63-linked polyubiquitin chains. These results mechanistically connect caspase-mediated cleavage and K63 ubiquitination in immune-induced NF-kappaB signaling.}, keywords = {Alleles, Amino Acid Motifs, Biological, Caspases, Inhibitor of Apoptosis Proteins, MAP Kinase Kinase Kinases, Models, NF-kappa B, Sequence Alignment, Signal Transduction, Ubiquitin-Protein Ligases, Ubiquitination}, pubstate = {published}, tppubtype = {article} } Innate immune responses are critical for the immediate protection against microbial infection. In Drosophila, infection leads to the rapid and robust production of antimicrobial peptides through two NF-kappaB signaling pathways-IMD and Toll. The IMD pathway is triggered by DAP-type peptidoglycan, common to most Gram-negative bacteria. Signaling downstream from the peptidoglycan receptors is thought to involve K63 ubiquitination and caspase-mediated cleavage, but the molecular mechanisms remain obscure. We now show that PGN stimulation causes caspase-mediated cleavage of the imd protein, exposing a highly conserved IAP-binding motif (IBM) at its neo-N terminus. A functional IBM is required for the association of cleaved IMD with the ubiquitin E3-ligase DIAP2. Through its association with DIAP2, IMD is rapidly conjugated with K63-linked polyubiquitin chains. These results mechanistically connect caspase-mediated cleavage and K63 ubiquitination in immune-induced NF-kappaB signaling. |
2009 |
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Articles de journaux |
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| 8. | Fraiture, Malou; Baxter, Richard H G; Steinert, Stefanie; Chelliah, Yogarany; Frolet, Cécile; Quispe-Tintaya, Wilber; Hoffmann, Jules A; Blandin, Stéphanie A; Levashina, Elena A Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium Article de journal Cell Host Microbe, 5 (3), p. 273–284, 2009, ISSN: 1934-6069. Résumé | Liens | BibTeX | Étiquettes: Anopheles, APL1, Biological, Complement System Proteins, Hemolymph, Immunologic Factors, LRIM1, Models, Plasmodium, Protein Binding, Proteins, TEP1 @article{fraiture_two_2009, title = {Two mosquito LRR proteins function as complement control factors in the TEP1-mediated killing of Plasmodium}, author = { Malou Fraiture and Richard H. G. Baxter and Stefanie Steinert and Yogarany Chelliah and Cécile Frolet and Wilber Quispe-Tintaya and Jules A. Hoffmann and Stéphanie A. Blandin and Elena A. Levashina}, doi = {10.1016/j.chom.2009.01.005}, issn = {1934-6069}, year = {2009}, date = {2009-03-01}, journal = {Cell Host Microbe}, volume = {5}, number = {3}, pages = {273--284}, abstract = {Plasmodium development within Anopheles mosquitoes is a vulnerable step in the parasite transmission cycle, and targeting this step represents a promising strategy for malaria control. The thioester-containing complement-like protein TEP1 and two leucine-rich repeat (LRR) proteins, LRIM1 and APL1, have been identified as major mosquito factors that regulate parasite loads. Here, we show that LRIM1 and APL1 are required for binding of TEP1 to parasites. RNAi silencing of the LRR-encoding genes results in deposition of TEP1 on Anopheles tissues, thereby depleting TEP1 from circulation in the hemolymph and impeding its binding to Plasmodium. LRIM1 and APL1 not only stabilize circulating TEP1, they also stabilize each other prior to their interaction with TEP1. Our results indicate that three major antiparasitic factors in mosquitoes jointly function as a complement-like system in parasite killing, and they reveal a role for LRR proteins as complement control factors.}, keywords = {Anopheles, APL1, Biological, Complement System Proteins, Hemolymph, Immunologic Factors, LRIM1, Models, Plasmodium, Protein Binding, Proteins, TEP1}, pubstate = {published}, tppubtype = {article} } Plasmodium development within Anopheles mosquitoes is a vulnerable step in the parasite transmission cycle, and targeting this step represents a promising strategy for malaria control. The thioester-containing complement-like protein TEP1 and two leucine-rich repeat (LRR) proteins, LRIM1 and APL1, have been identified as major mosquito factors that regulate parasite loads. Here, we show that LRIM1 and APL1 are required for binding of TEP1 to parasites. RNAi silencing of the LRR-encoding genes results in deposition of TEP1 on Anopheles tissues, thereby depleting TEP1 from circulation in the hemolymph and impeding its binding to Plasmodium. LRIM1 and APL1 not only stabilize circulating TEP1, they also stabilize each other prior to their interaction with TEP1. Our results indicate that three major antiparasitic factors in mosquitoes jointly function as a complement-like system in parasite killing, and they reveal a role for LRR proteins as complement control factors. |
2006 |
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Articles de journaux |
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| 7. | Chen, Li-Ying; Wang, Juinn-Chin; Hyvert, Yann; Lin, Hui-Ping; Perrimon, Norbert; Imler, Jean-Luc; Hsu, Jui-Chou Weckle is a zinc finger adaptor of the toll pathway in dorsoventral patterning of the Drosophila embryo Article de journal Current biology: CB, 16 (12), p. 1183–1193, 2006, ISSN: 0960-9822. Résumé | Liens | BibTeX | Étiquettes: Adaptor Proteins, Antigens, Biological, Body Patterning, Cell Membrane, Differentiation, Dimerization, DNA-Binding Proteins, Embryo, Epistasis, Genetic, Immunity, Immunologic, Innate, Models, Mutation, Nonmammalian, Phenotype, Phosphoproteins, Receptors, Signal Transducing, Toll-Like Receptors, Transcription Factors, Zinc Fingers @article{chen_weckle_2006, title = {Weckle is a zinc finger adaptor of the toll pathway in dorsoventral patterning of the Drosophila embryo}, author = { Li-Ying Chen and Juinn-Chin Wang and Yann Hyvert and Hui-Ping Lin and Norbert Perrimon and Jean-Luc Imler and Jui-Chou Hsu}, doi = {10.1016/j.cub.2006.05.050}, issn = {0960-9822}, year = {2006}, date = {2006-06-01}, journal = {Current biology: CB}, volume = {16}, number = {12}, pages = {1183--1193}, abstract = {BACKGROUND: The Drosophila Toll pathway takes part in both establishment of the embryonic dorsoventral axis and induction of the innate immune response in adults. Upon activation by the cytokine Spätzle, Toll interacts with the adaptor proteins DmMyD88 and Tube and the kinase Pelle and triggers degradation of the inhibitor Cactus, thus allowing the nuclear translocation of the transcription factor Dorsal/Dif. weckle (wek) was previously identified as a new dorsal group gene that encodes a putative zinc finger transcription factor. However, its role in the Toll pathway was unknown. RESULTS: Here, we isolated new wek alleles and demonstrated that cactus is epistatic to wek, which in turn is epistatic to Toll. Consistent with this, Wek localizes to the plasma membrane of embryos, independently of Toll signaling. Wek homodimerizes and associates with Toll. Moreover, Wek binds to and localizes DmMyD88 to the plasma membrane. Thus, Wek acts as an adaptor to assemble/stabilize a Toll/Wek/DmMyD88/Tube complex. Remarkably, unlike the DmMyD88/tube/pelle/cactus gene cassette of the Toll pathway, wek plays a minimal role, if any, in the immune defense against Gram-positive bacteria and fungi. CONCLUSIONS: We conclude that Wek is an adaptor to link Toll and DmMyD88 and is required for efficient recruitment of DmMyD88 to Toll. Unexpectedly, wek is dispensable for innate immune response, thus revealing differences in the Toll-mediated activation of Dorsal in the embryo and Dif in the fat body of adult flies.}, keywords = {Adaptor Proteins, Antigens, Biological, Body Patterning, Cell Membrane, Differentiation, Dimerization, DNA-Binding Proteins, Embryo, Epistasis, Genetic, Immunity, Immunologic, Innate, Models, Mutation, Nonmammalian, Phenotype, Phosphoproteins, Receptors, Signal Transducing, Toll-Like Receptors, Transcription Factors, Zinc Fingers}, pubstate = {published}, tppubtype = {article} } BACKGROUND: The Drosophila Toll pathway takes part in both establishment of the embryonic dorsoventral axis and induction of the innate immune response in adults. Upon activation by the cytokine Spätzle, Toll interacts with the adaptor proteins DmMyD88 and Tube and the kinase Pelle and triggers degradation of the inhibitor Cactus, thus allowing the nuclear translocation of the transcription factor Dorsal/Dif. weckle (wek) was previously identified as a new dorsal group gene that encodes a putative zinc finger transcription factor. However, its role in the Toll pathway was unknown. RESULTS: Here, we isolated new wek alleles and demonstrated that cactus is epistatic to wek, which in turn is epistatic to Toll. Consistent with this, Wek localizes to the plasma membrane of embryos, independently of Toll signaling. Wek homodimerizes and associates with Toll. Moreover, Wek binds to and localizes DmMyD88 to the plasma membrane. Thus, Wek acts as an adaptor to assemble/stabilize a Toll/Wek/DmMyD88/Tube complex. Remarkably, unlike the DmMyD88/tube/pelle/cactus gene cassette of the Toll pathway, wek plays a minimal role, if any, in the immune defense against Gram-positive bacteria and fungi. CONCLUSIONS: We conclude that Wek is an adaptor to link Toll and DmMyD88 and is required for efficient recruitment of DmMyD88 to Toll. Unexpectedly, wek is dispensable for innate immune response, thus revealing differences in the Toll-mediated activation of Dorsal in the embryo and Dif in the fat body of adult flies. |
2000 |
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Articles de journaux |
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| 6. | Imler, Jean-Luc; Tauszig, Servane ; Jouanguy, Emmanuelle ; Forestier, C; Hoffmann, Jules A LPS-induced immune response in Drosophila Article de journal Journal of Endotoxin Research, 6 (6), p. 459–462, 2000, ISSN: 0968-0519. Résumé | BibTeX | Étiquettes: Biological, Cell Line, Cell Surface, Defensins, Genes, Genetic, Insect, Insect Proteins, Lipopolysaccharides, Membrane Glycoproteins, Models, Mutation, Promoter Regions, Receptors, Signal Transduction, Toll-Like Receptors @article{imler_lps-induced_2000, title = {LPS-induced immune response in Drosophila}, author = { Jean-Luc Imler and Servane Tauszig and Emmanuelle Jouanguy and C. Forestier and Jules A. Hoffmann}, issn = {0968-0519}, year = {2000}, date = {2000-01-01}, journal = {Journal of Endotoxin Research}, volume = {6}, number = {6}, pages = {459--462}, abstract = {The study of the regulation of the inducible synthesis of antimicrobial peptides in Drosophila melanogaster has established this insect as a powerful model in which to study innate immunity. In particular, the molecular characterization of the regulatory pathway controlling the antifungal peptide drosomycin has revealed the importance of Toll receptors in innate immunity. We report here that injection of LPS into flies induces an immune response, suggesting that LPS receptors are used in Drosophila to detect Gram-negative bacteria infection. We have identified in the recently sequenced genome of Drosophila eight genes coding for Toll-like receptors in addition to Toll, which may function as LPS receptors. However, overexpression of a selection of these genes in tissue-culture cells does not result in up-regulation of the antibacterial peptide genes. These results are discussed in light of the recent data from genetic screens aimed at identifying the genes controlling the antibacterial response in Drosophila.}, keywords = {Biological, Cell Line, Cell Surface, Defensins, Genes, Genetic, Insect, Insect Proteins, Lipopolysaccharides, Membrane Glycoproteins, Models, Mutation, Promoter Regions, Receptors, Signal Transduction, Toll-Like Receptors}, pubstate = {published}, tppubtype = {article} } The study of the regulation of the inducible synthesis of antimicrobial peptides in Drosophila melanogaster has established this insect as a powerful model in which to study innate immunity. In particular, the molecular characterization of the regulatory pathway controlling the antifungal peptide drosomycin has revealed the importance of Toll receptors in innate immunity. We report here that injection of LPS into flies induces an immune response, suggesting that LPS receptors are used in Drosophila to detect Gram-negative bacteria infection. We have identified in the recently sequenced genome of Drosophila eight genes coding for Toll-like receptors in addition to Toll, which may function as LPS receptors. However, overexpression of a selection of these genes in tissue-culture cells does not result in up-regulation of the antibacterial peptide genes. These results are discussed in light of the recent data from genetic screens aimed at identifying the genes controlling the antibacterial response in Drosophila. |
1988 |
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Articles de journaux |
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| 5. | Kappler, Christine; Kabbouh, M; Hetru, Charles; Durst, F; Hoffmann, Jules A Characterization of three hydroxylases involved in the final steps of biosynthesis of the steroid hormone ecdysone in Locusta migratoria (Insecta, Orthoptera) Article de journal J. Steroid Biochem., 31 (6), p. 891–898, 1988, ISSN: 0022-4731. Résumé | BibTeX | Étiquettes: Biological, Ecdysone, Grasshoppers, Kinetics, Mixed Function Oxygenases, Models, NAD, NADP, Subcellular Fractions @article{kappler_characterization_1988, title = {Characterization of three hydroxylases involved in the final steps of biosynthesis of the steroid hormone ecdysone in Locusta migratoria (Insecta, Orthoptera)}, author = { Christine Kappler and M. Kabbouh and Charles Hetru and F. Durst and Jules A. Hoffmann}, issn = {0022-4731}, year = {1988}, date = {1988-12-01}, journal = {J. Steroid Biochem.}, volume = {31}, number = {6}, pages = {891--898}, abstract = {It is most generally accepted that the last three enzymatic reactions in the biosynthetic pathway of ecdysone are, in this order, the hydroxylations at positions C-25, C-22 and C-2. Using high specific activity tritiated ecdysone precursors (2,22,25-trideoxyecdysone, 2,22-dideoxyecdysone and 2-deoxyecdysone) we have characterized the hydroxylases involved in these reactions, in the major biosynthetic tissue of ecdysone, i.e. the prothoracic glands. We show that C-2 hydroxylase is a mitochondrial oxygenase which differs from conventional cytochrome P-450-dependent monooxygenases by its relative insensitivity to CO. In contrast, C-22 and C-25 hydroxylases appear as classical cytochrome P-450 monooxygenases; C-22 hydroxylase is a mitochondrial enzyme whereas our data point to a microsomal localization of the C-25 hydroxylase.}, keywords = {Biological, Ecdysone, Grasshoppers, Kinetics, Mixed Function Oxygenases, Models, NAD, NADP, Subcellular Fractions}, pubstate = {published}, tppubtype = {article} } It is most generally accepted that the last three enzymatic reactions in the biosynthetic pathway of ecdysone are, in this order, the hydroxylations at positions C-25, C-22 and C-2. Using high specific activity tritiated ecdysone precursors (2,22,25-trideoxyecdysone, 2,22-dideoxyecdysone and 2-deoxyecdysone) we have characterized the hydroxylases involved in these reactions, in the major biosynthetic tissue of ecdysone, i.e. the prothoracic glands. We show that C-2 hydroxylase is a mitochondrial oxygenase which differs from conventional cytochrome P-450-dependent monooxygenases by its relative insensitivity to CO. In contrast, C-22 and C-25 hydroxylases appear as classical cytochrome P-450 monooxygenases; C-22 hydroxylase is a mitochondrial enzyme whereas our data point to a microsomal localization of the C-25 hydroxylase. |
1980 |
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Articles de journaux |
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| 4. | Zachary, Daniel; Hoffmann, Jules A Endocrine control of the metamorphosis of the larval muscles in Calliphora erythrocephala (Diptera): in vitro studies of the role of ecdysteroids Article de journal Dev. Biol., 80 (1), p. 235–247, 1980, ISSN: 0012-1606. BibTeX | Étiquettes: Biological, Diptera, Ecdysone, Ecdysterone, Larva, Metamorphosis, Muscles, Organ Culture Techniques @article{zachary_endocrine_1980, title = {Endocrine control of the metamorphosis of the larval muscles in Calliphora erythrocephala (Diptera): in vitro studies of the role of ecdysteroids}, author = { Daniel Zachary and Jules A. Hoffmann}, issn = {0012-1606}, year = {1980}, date = {1980-11-01}, journal = {Dev. Biol.}, volume = {80}, number = {1}, pages = {235--247}, keywords = {Biological, Diptera, Ecdysone, Ecdysterone, Larva, Metamorphosis, Muscles, Organ Culture Techniques}, pubstate = {published}, tppubtype = {article} } |
1973 |
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Articles de journaux |
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| 3. | Koolman, J; Hoffmann, Jules A; Karlson, P Sulphage esters as inactivation products of ecdysone in Locusta migratoria Article de journal Hoppe-Seyler's Z. Physiol. Chem., 354 (9), p. 1043–1048, 1973, ISSN: 0018-4888. BibTeX | Étiquettes: Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium @article{koolman_sulphage_1973, title = {Sulphage esters as inactivation products of ecdysone in Locusta migratoria}, author = { J. Koolman and Jules A. Hoffmann and P. Karlson}, issn = {0018-4888}, year = {1973}, date = {1973-09-01}, journal = {Hoppe-Seyler's Z. Physiol. Chem.}, volume = {354}, number = {9}, pages = {1043--1048}, keywords = {Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium}, pubstate = {published}, tppubtype = {article} } |
| 2. | Joly, L; Weins, M J; Hoffmann, Jules A; Porte, A Development of the prothoracic glands of permanent larvae of Locusta migratoria obtained by selective irradiation of the hemocytopoietic tissue Article de journal Z Zellforsch Mikrosk Anat, 137 (3), p. 387–397, 1973, ISSN: 0340-0336. BibTeX | Étiquettes: Age Factors, Biological, Ecdysone, Electron, Endocrine Glands, Golgi Apparatus, Grasshoppers, Larva, Metamorphosis, Microscopy, Radiation Effects, Ribosomes @article{joly_development_1973, title = {Development of the prothoracic glands of permanent larvae of Locusta migratoria obtained by selective irradiation of the hemocytopoietic tissue}, author = { L. Joly and M. J. Weins and Jules A. Hoffmann and A. Porte}, issn = {0340-0336}, year = {1973}, date = {1973-02-01}, journal = {Z Zellforsch Mikrosk Anat}, volume = {137}, number = {3}, pages = {387--397}, keywords = {Age Factors, Biological, Ecdysone, Electron, Endocrine Glands, Golgi Apparatus, Grasshoppers, Larva, Metamorphosis, Microscopy, Radiation Effects, Ribosomes}, pubstate = {published}, tppubtype = {article} } |
1970 |
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Articles de journaux |
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| 1. | Hoffmann, Jules A Endocrine regulation of production and differentiation of hemocytes in an orthopteran insect: Locusta migratoria migratoroides Article de journal Gen. Comp. Endocrinol., 15 (2), p. 198–219, 1970, ISSN: 0016-6480. BibTeX | Étiquettes: Biological, Blood Cells, Electrocoagulation, Female, Hemolymph, Insects, Male, Metamorphosis, Microscopy, Neurosecretory Systems, Phase-Contrast @article{hoffmann_endocrine_1970, title = {Endocrine regulation of production and differentiation of hemocytes in an orthopteran insect: Locusta migratoria migratoroides}, author = { Jules A. Hoffmann}, issn = {0016-6480}, year = {1970}, date = {1970-10-01}, journal = {Gen. Comp. Endocrinol.}, volume = {15}, number = {2}, pages = {198--219}, keywords = {Biological, Blood Cells, Electrocoagulation, Female, Hemolymph, Insects, Male, Metamorphosis, Microscopy, Neurosecretory Systems, Phase-Contrast}, pubstate = {published}, tppubtype = {article} } |
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