Publications
2003 |
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3. | 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 Article de journal Science, 302 (5653), p. 2126–2130, 2003, ISSN: 1095-9203. Résumé | Liens | BibTeX | Étiquettes: Carrier Proteins, Cell Surface, DNA Transposable Elements, Gene Expression, Genes, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolymph, Hypocreales, Insect, Insect Proteins, 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 = {Carrier Proteins, Cell Surface, DNA Transposable Elements, Gene Expression, Genes, Gram-Negative Bacteria, Gram-Positive Bacteria, Hemolymph, Hypocreales, Insect, Insect Proteins, Mutation, Phenotype, Receptors, Serine Endopeptidases, Toll-Like Receptors}, pubstate = {published}, tppubtype = {article} } 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. |
2002 |
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Articles de journaux |
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2. | Ligoxygakis, Petros; Pelte, Nadège ; Hoffmann, Jules A; Reichhart, Jean-Marc Activation of Drosophila Toll during fungal infection by a blood serine protease Article de journal Science, 297 (5578), p. 114–116, 2002, ISSN: 1095-9203. Résumé | Liens | BibTeX | Étiquettes: Cell Surface, Chromosome Mapping, Escherichia coli, Female, Gene Expression Regulation, Genes, Gram-Positive Cocci, Hemolymph, Hypocreales, Insect, Insect Proteins, Male, Mutation, Protein Sorting Signals, Protein Structure, Receptors, Serine Endopeptidases, Tertiary, Toll-Like Receptors @article{ligoxygakis_activation_2002, title = {Activation of Drosophila Toll during fungal infection by a blood serine protease}, author = { Petros Ligoxygakis and Nadège Pelte and Jules A. Hoffmann and Jean-Marc Reichhart}, doi = {10.1126/science.1072391}, issn = {1095-9203}, year = {2002}, date = {2002-07-01}, journal = {Science}, volume = {297}, number = {5578}, pages = {114--116}, abstract = {Drosophila host defense to fungal and Gram-positive bacterial infection is mediated by the Spaetzle/Toll/cactus gene cassette. It has been proposed that Toll does not function as a pattern recognition receptor per se but is activated through a cleaved form of the cytokine Spaetzle. The upstream events linking infection to the cleavage of Spaetzle have long remained elusive. Here we report the identification of a central component of the fungal activation of Toll. We show that ethylmethane sulfonate-induced mutations in the persephone gene, which encodes a previously unknown serine protease, block induction of the Toll pathway by fungi and resistance to this type of infection.}, keywords = {Cell Surface, Chromosome Mapping, Escherichia coli, Female, Gene Expression Regulation, Genes, Gram-Positive Cocci, Hemolymph, Hypocreales, Insect, Insect Proteins, Male, Mutation, Protein Sorting Signals, Protein Structure, Receptors, Serine Endopeptidases, Tertiary, Toll-Like Receptors}, pubstate = {published}, tppubtype = {article} } Drosophila host defense to fungal and Gram-positive bacterial infection is mediated by the Spaetzle/Toll/cactus gene cassette. It has been proposed that Toll does not function as a pattern recognition receptor per se but is activated through a cleaved form of the cytokine Spaetzle. The upstream events linking infection to the cleavage of Spaetzle have long remained elusive. Here we report the identification of a central component of the fungal activation of Toll. We show that ethylmethane sulfonate-induced mutations in the persephone gene, which encodes a previously unknown serine protease, block induction of the Toll pathway by fungi and resistance to this type of infection. |
1. | Tauszig-Delamasure, Servane; Bilak, Hana ; Capovilla, Maria ; Hoffmann, Jules A; Imler, Jean-Luc Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections Article de journal Nature Immunology, 3 (1), p. 91–97, 2002, ISSN: 1529-2908. Résumé | Liens | BibTeX | Étiquettes: Adaptor Proteins, Amino Acid, Antigens, Antimicrobial Cationic Peptides, Cell Surface, Chromosome Mapping, Differentiation, Disease Susceptibility, Enterococcus faecalis, Epistasis, Escherichia coli, Female, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Gram-Negative Bacteria, Hypocreales, Immunologic, Insect, Insect Proteins, Membrane Glycoproteins, Micrococcus luteus, Myeloid Differentiation Factor 88, Protein Structure, Protein-Serine-Threonine Kinases, Receptors, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Signal Transducing, Tertiary, Toll-Like Receptors, Transfection @article{tauszig-delamasure_drosophila_2002, title = {Drosophila MyD88 is required for the response to fungal and Gram-positive bacterial infections}, author = { Servane Tauszig-Delamasure and Hana Bilak and Maria Capovilla and Jules A. Hoffmann and Jean-Luc Imler}, doi = {10.1038/ni747}, issn = {1529-2908}, year = {2002}, date = {2002-01-01}, journal = {Nature Immunology}, volume = {3}, number = {1}, pages = {91--97}, abstract = {We report here the identification and functional characterization of DmMyD88, a gene encoding the Drosophila homolog of mammalian MyD88. DmMyD88 combines a Toll-IL-1R homology (TIR) domain and a death domain. Overexpression of DmMyD88 was sufficient to induce expression of the antifungal peptide Drosomycin, and induction of Drosomycin was markedly reduced in DmMyD88-mutant flies. DmMyD88 interacted with Toll through its TIR domain and required the death domain proteins Tube and Pelle to activate expression of Drs, which encodes Drosomycin. DmMyD88-mutant flies were highly susceptible to infection by fungi and Gram-positive bacteria, but resisted Gram-negative bacterial infection much as did wild-type flies. Phenotypic comparison of DmMyD88-mutant flies and MyD88-deficient mice showed essential differences in the control of Gram-negative infection in insects and mammals.}, keywords = {Adaptor Proteins, Amino Acid, Antigens, Antimicrobial Cationic Peptides, Cell Surface, Chromosome Mapping, Differentiation, Disease Susceptibility, Enterococcus faecalis, Epistasis, Escherichia coli, Female, Gene Expression Regulation, Genes, Genetic, Genetically Modified, Gram-Negative Bacteria, Hypocreales, Immunologic, Insect, Insect Proteins, Membrane Glycoproteins, Micrococcus luteus, Myeloid Differentiation Factor 88, Protein Structure, Protein-Serine-Threonine Kinases, Receptors, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Signal Transducing, Tertiary, Toll-Like Receptors, Transfection}, pubstate = {published}, tppubtype = {article} } We report here the identification and functional characterization of DmMyD88, a gene encoding the Drosophila homolog of mammalian MyD88. DmMyD88 combines a Toll-IL-1R homology (TIR) domain and a death domain. Overexpression of DmMyD88 was sufficient to induce expression of the antifungal peptide Drosomycin, and induction of Drosomycin was markedly reduced in DmMyD88-mutant flies. DmMyD88 interacted with Toll through its TIR domain and required the death domain proteins Tube and Pelle to activate expression of Drs, which encodes Drosomycin. DmMyD88-mutant flies were highly susceptible to infection by fungi and Gram-positive bacteria, but resisted Gram-negative bacterial infection much as did wild-type flies. Phenotypic comparison of DmMyD88-mutant flies and MyD88-deficient mice showed essential differences in the control of Gram-negative infection in insects and mammals. |
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