Publications
2012
Coste Franck, Kemp Cordula, Bobezeau Vanessa, Hetru Charles, Kellenberger Christine, Imler Jean-Luc, Roussel Alain
Crystal structure of Diedel, a marker of the immune response of Drosophila melanogaster Article de journal
Dans: PloS One, vol. 7, no. 3, p. e33416, 2012, ISSN: 1932-6203.
Résumé | Liens | BibTeX | Étiquettes: Animals, Aphids, Crystallography, imler, Janus Kinases, M3i, Protein Folding, Protein Structure, Signal Transduction, STAT Transcription Factors, Tertiary, Transcription Factors, X-Ray
@article{coste_crystal_2012,
title = {Crystal structure of Diedel, a marker of the immune response of Drosophila melanogaster},
author = {Franck Coste and Cordula Kemp and Vanessa Bobezeau and Charles Hetru and Christine Kellenberger and Jean-Luc Imler and Alain Roussel},
doi = {10.1371/journal.pone.0033416},
issn = {1932-6203},
year = {2012},
date = {2012-01-01},
journal = {PloS One},
volume = {7},
number = {3},
pages = {e33416},
abstract = {BACKGROUND: The Drosophila melanogaster gene CG11501 is up regulated after a septic injury and was proposed to act as a negative regulator of the JAK/STAT signaling pathway. Diedel, the CG11501 gene product, is a small protein of 115 residues with 10 cysteines. METHODOLOGY/PRINCIPAL FINDINGS: We have produced Diedel in Drosophila S2 cells as an extra cellular protein thanks to its own signal peptide and solved its crystal structure at 1.15 Å resolution by SIRAS using an iodo derivative. Diedel is composed of two sub domains SD1 and SD2. SD1 is made of an antiparallel β-sheet covered by an α-helix and displays a ferredoxin-like fold. SD2 reveals a new protein fold made of loops connected by four disulfide bridges. Further structural analysis identified conserved hydrophobic residues on the surface of Diedel that may constitute a potential binding site. The existence of two conformations, cis and trans, for the proline 52 may be of interest as prolyl peptidyl isomerisation has been shown to play a role in several physiological mechanisms. The genome of D. melanogaster contains two other genes coding for proteins homologous to Diedel, namely CG43228 and CG34329. Strikingly, apart from Drosophila and the pea aphid Acyrthosiphon pisum, Diedel-related sequences were exclusively identified in a few insect DNA viruses of the Baculoviridae and Ascoviridae families. CONCLUSION/SIGNIFICANCE: Diedel, a marker of the Drosophila antimicrobial/antiviral response, is a member of a small family of proteins present in drosophilids, aphids and DNA viruses infecting lepidopterans. Diedel is an extracellular protein composed of two sub-domains. Two special structural features (hydrophobic surface patch and cis/trans conformation for proline 52) may indicate a putative interaction site, and support an extra cellular signaling function for Diedel, which is in accordance with its proposed role as negative regulator of the JAK/STAT signaling pathway.},
keywords = {Animals, Aphids, Crystallography, imler, Janus Kinases, M3i, Protein Folding, Protein Structure, Signal Transduction, STAT Transcription Factors, Tertiary, Transcription Factors, X-Ray},
pubstate = {published},
tppubtype = {article}
}
2010
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
Dans: J. Biol. Chem., vol. 285, no. 32, p. 24307–24312, 2010, ISSN: 1083-351X.
Résumé | Liens | BibTeX | Étiquettes: Animals, Biological, Biological Transport, Biophysics, Catalytic Domain, Hormones, Humans, Kinetics, M3i, Models, Peptide Hydrolases, Protein Binding, Protein Conformation, Protein Structure, reichhart, 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 = {Animals, Biological, Biological Transport, Biophysics, Catalytic Domain, Hormones, Humans, Kinetics, M3i, Models, Peptide Hydrolases, Protein Binding, Protein Conformation, Protein Structure, reichhart, Serpins, Substrate Specificity, Tertiary, Thrombin},
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 Article de journal
Dans: J. Biol. Chem., vol. 284, no. 42, p. 28687–28697, 2009, ISSN: 1083-351X.
Résumé | Liens | BibTeX | Étiquettes: 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}
}
2007
Weber Alexander N R, Gangloff Monique, Moncrieffe Martin C, Hyvert Yann, Imler Jean-Luc, Gay Nicholas J
Role of the Spatzle Pro-domain in the generation of an active toll receptor ligand Article de journal
Dans: The Journal of Biological Chemistry, vol. 282, no. 18, p. 13522–13531, 2007, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Animals, Cytokines, dimerization, imler, ligands, M3i, Post-Translational, Protein Binding, Protein Processing, Protein Structure, Signal Transduction, Tertiary, Toll-Like Receptors
@article{weber_role_2007,
title = {Role of the Spatzle Pro-domain in the generation of an active toll receptor ligand},
author = {Alexander N R Weber and Monique Gangloff and Martin C Moncrieffe and Yann Hyvert and Jean-Luc Imler and Nicholas J Gay},
doi = {10.1074/jbc.M700068200},
issn = {0021-9258},
year = {2007},
date = {2007-05-01},
journal = {The Journal of Biological Chemistry},
volume = {282},
number = {18},
pages = {13522--13531},
abstract = {The cytokine Spätzle is the ligand for Drosophila Toll, the prototype of an important family of membrane receptors that function in embryonic patterning and innate immunity. A dimeric precursor of Spätzle is processed by an endoprotease to produce a form (C-106) that cross-links Toll receptor ectodomains and establishes signaling. Here we show that before processing the pro-domain of Spätzle is required for correct biosynthesis and secretion. We mapped two loss-of-function mutations of Spätzle to a discrete site in the pro-domain and showed that the phenotype arises because of a defect in biosynthesis rather than signaling. We also report that the pro-domain and C-106 remain associated after cleavage and that this processed complex signals with the same characteristics as the C-terminal fragment. These results suggest that before activation the determinants on C-106 that bind specifically to Toll are sequestered by the pro-domain and that proteolytic processing causes conformational rearrangements that expose these determinants and enables binding to Toll. Furthermore, we show that the pro-domain is released when the Toll extracellular domain binds to the complex, a finding that has implications for the generation of a signaling-competent Toll dimer.},
keywords = {Animals, Cytokines, dimerization, imler, ligands, M3i, Post-Translational, Protein Binding, Protein Processing, Protein Structure, Signal Transduction, Tertiary, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
2005
Weber Alexander N R, Moncrieffe Martin C, Gangloff Monique, Imler Jean-Luc, Gay Nicholas J
Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway Article de journal
Dans: The Journal of Biological Chemistry, vol. 280, no. 24, p. 22793–22799, 2005, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation
@article{weber_ligand-receptor_2005,
title = {Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway},
author = {Alexander N R Weber and Martin C Moncrieffe and Monique Gangloff and Jean-Luc Imler and Nicholas J Gay},
doi = {10.1074/jbc.M502074200},
issn = {0021-9258},
year = {2005},
date = {2005-01-01},
journal = {The Journal of Biological Chemistry},
volume = {280},
number = {24},
pages = {22793--22799},
abstract = {In Drosophila, the signaling pathway mediated by the Toll receptor is critical for the establishment of embryonic dorso-ventral pattern and for innate immune responses to bacterial and fungal pathogens. Toll is activated by high affinity binding of the cytokine Spätzle, a dimeric ligand of the cystine knot family. In vertebrates, a related family of Toll-like receptors play a critical role in innate immune responses. Despite the importance of this family of receptors, little is known about the biochemical events that lead to receptor activation and signaling. Here, we show that Spätzle binds to the N-terminal region of Toll and, using biophysical methods, that the binding is complex. The two binding events that cause formation of the cross-linked complex are non-equivalent: the first Toll ectodomain binds Spätzle with an affinity 3-fold higher than the second molecule suggesting that pathway activation involves negative cooperativity. We further show that the Toll ectodomains are able to form low affinity dimers in solution and that juxtamembrane sequences of Toll are critical for the activation or derepression of the pathway. These results, taken together, suggest a mechanism of signal transduction that requires both ligand-receptor and receptor-receptor interactions.},
keywords = {Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation},
pubstate = {published},
tppubtype = {article}
}
2004
Blandin Stephanie A, Shiao Shin-Hong, Moita Luis F, Janse Chris J, Waters Andrew P, Kafatos Fotis C, Levashina Elena A
Complement-like protein TEP1 is a determinant of vectorial capacity in the malaria vector Anopheles gambiae Article de journal
Dans: Cell, vol. 116, no. 5, p. 661–670, 2004, ISSN: 0092-8674.
Résumé | BibTeX | Étiquettes: Animals, Anopheles, blandin, Female, Genetic, Humans, Insect Proteins, Insect Vectors, M3i, Malaria, Models, Molecular, Plasmodium berghei, Polymorphism, Protein Structure, RNA, Sequence Alignment, Tertiary
@article{blandin_complement-like_2004,
title = {Complement-like protein TEP1 is a determinant of vectorial capacity in the malaria vector Anopheles gambiae},
author = {Stephanie A Blandin and Shin-Hong Shiao and Luis F Moita and Chris J Janse and Andrew P Waters and Fotis C Kafatos and Elena A Levashina},
issn = {0092-8674},
year = {2004},
date = {2004-01-01},
journal = {Cell},
volume = {116},
number = {5},
pages = {661--670},
abstract = {Anopheles mosquitoes are major vectors of human malaria in Africa. Large variation exists in the ability of mosquitoes to serve as vectors and to transmit malaria parasites, but the molecular mechanisms that determine vectorial capacity remain poorly understood. We report that the hemocyte-specific complement-like protein TEP1 from the mosquito Anopheles gambiae binds to and mediates killing of midgut stages of the rodent malaria parasite Plasmodium berghei. The dsRNA knockdown of TEP1 in adults completely abolishes melanotic refractoriness in a genetically selected refractory strain. Moreover, in susceptible mosquitoes this knockdown increases the number of developing parasites. Our results suggest that the TEP1-dependent parasite killing is followed by a TEP1-independent clearance of dead parasites by lysis and/or melanization. Further elucidation of the molecular mechanisms of TEP1-mediated parasite killing will be of great importance for our understanding of the principles of vectorial capacity in insects.},
keywords = {Animals, Anopheles, blandin, Female, Genetic, Humans, Insect Proteins, Insect Vectors, M3i, Malaria, Models, Molecular, Plasmodium berghei, Polymorphism, Protein Structure, RNA, Sequence Alignment, Tertiary},
pubstate = {published},
tppubtype = {article}
}
2003
Bianco Alberto, Pantarotto Davide, Hoebeke Johan, Briand Jean-Paul, Prato Maurizio
Solid-phase synthesis and characterization of a novel fullerene-peptide derived from histone H3 Article de journal
Dans: Organic & Biomolecular Chemistry, vol. 1, no. 23, p. 4141–4143, 2003, ISSN: 1477-0520.
Résumé | Liens | BibTeX | Étiquettes: Chromatography, Epitopes, Fullerenes, Glutamic Acid, High Pressure Liquid, Histones, I2CT, Models, Molecular, Molecular Structure, Peptides, Protein Structure, Team-Bianco, Tertiary
@article{bianco_solid-phase_2003,
title = {Solid-phase synthesis and characterization of a novel fullerene-peptide derived from histone H3},
author = {Alberto Bianco and Davide Pantarotto and Johan Hoebeke and Jean-Paul Briand and Maurizio Prato},
doi = {10.1039/b311505d},
issn = {1477-0520},
year = {2003},
date = {2003-12-01},
journal = {Organic & Biomolecular Chemistry},
volume = {1},
number = {23},
pages = {4141--4143},
abstract = {A peptide analogue from a histone H3 protein containing the L-fulleropyrrolidino-glutamic acid has been prepared by a solid-phase approach and has been fully characterized. By molecular modelling it was verified that this peptide derivative is able to retain a binding capacity to the MHC (major histocompatibility complex) molecule similar to that of the cognate epitope.},
keywords = {Chromatography, Epitopes, Fullerenes, Glutamic Acid, High Pressure Liquid, Histones, I2CT, Models, Molecular, Molecular Structure, Peptides, Protein Structure, Team-Bianco, Tertiary},
pubstate = {published},
tppubtype = {article}
}
Weber Alexander N R, Tauszig-Delamasure Servane, Hoffmann Jules A, Lelièvre Eric, Gascan Hugues, Ray Keith P, Morse Mary A, Imler Jean-Luc, Gay Nicholas J
Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling Article de journal
Dans: Nature Immunology, vol. 4, no. 8, p. 794–800, 2003, ISSN: 1529-2908.
Résumé | Liens | BibTeX | Étiquettes: Animals, Cell Surface, hoffmann, imler, Insect Proteins, M3i, Protein Binding, Protein Structure, Receptors, Signal Transduction, Tertiary, Toll-Like Receptors
@article{weber_binding_2003,
title = {Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling},
author = {Alexander N R Weber and Servane Tauszig-Delamasure and Jules A Hoffmann and Eric Lelièvre and Hugues Gascan and Keith P Ray and Mary A Morse and Jean-Luc Imler and Nicholas J Gay},
doi = {10.1038/ni955},
issn = {1529-2908},
year = {2003},
date = {2003-08-01},
journal = {Nature Immunology},
volume = {4},
number = {8},
pages = {794--800},
abstract = {The extracellular protein Spätzle is required for activation of the Toll signaling pathway in the embryonic development and innate immune defense of Drosophila. Spätzle is synthesized as a pro-protein and is processed to a functional form by a serine protease. We show here that the mature form of Spätzle triggers a Toll-dependent immune response after injection into the hemolymph of flies. Spätzle specifically bound to Drosophila cells and to Cos-7 cells expressing Toll. Furthermore, in vitro experiments showed that the mature form of Spätzle bound to the Toll ectodomain with high affinity and with a stoichiometry of one Spätzle dimer to two receptors. The Spätzle pro-protein was inactive in all these assays, indicating that the pro-domain sequence, which is natively unstructured, acts to prevent interaction of the cytokine and its receptor Toll. These results show that, in contrast to the human Toll-like receptors, Drosophila Toll requires only an endogenous protein ligand for activation and signaling.},
keywords = {Animals, Cell Surface, hoffmann, imler, Insect Proteins, M3i, Protein Binding, Protein Structure, Receptors, Signal Transduction, Tertiary, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Imler Jean-Luc, Hoffmann Jules A
Toll signaling: the TIReless quest for specificity Article de journal
Dans: Nature Immunology, vol. 4, no. 2, p. 105–106, 2003, ISSN: 1529-2908.
Liens | BibTeX | Étiquettes: Animals, Cell Surface, Dendritic Cells, hoffmann, Humans, imler, Immunological, Interferon-beta, M3i, Membrane Glycoproteins, Mice, Models, Protein Structure, Receptors, Signal Transduction, Tertiary, Toll-Like Receptors
@article{imler_toll_2003,
title = {Toll signaling: the TIReless quest for specificity},
author = {Jean-Luc Imler and Jules A Hoffmann},
doi = {10.1038/ni0203-105},
issn = {1529-2908},
year = {2003},
date = {2003-02-01},
journal = {Nature Immunology},
volume = {4},
number = {2},
pages = {105--106},
keywords = {Animals, Cell Surface, Dendritic Cells, hoffmann, Humans, imler, Immunological, Interferon-beta, M3i, Membrane Glycoproteins, Mice, Models, Protein Structure, Receptors, Signal Transduction, Tertiary, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
Kambris Zakaria, Bilak Hana, D'Alessandro Rosalba, Belvin Marcia, Imler Jean-Luc, Capovilla Maria
DmMyD88 controls dorsoventral patterning of the Drosophila embryo Article de journal
Dans: EMBO reports, vol. 4, no. 1, p. 64–69, 2003, ISSN: 1469-221X.
Résumé | Liens | BibTeX | Étiquettes: Adaptor Proteins, Alleles, Animals, Antigens, Base Sequence, Cell Surface, Complementary, Developmental, Differentiation, DNA, DNA Transposable Elements, Egg Proteins, Embryo, Exons, Female, Gene Expression Regulation, Genetically Modified, Genotype, imler, Immunity, Immunologic, Innate, Insertional, M3i, Male, messenger, Morphogenesis, Mutagenesis, Myeloid Differentiation Factor 88, Nonmammalian, Oocytes, Protein Biosynthesis, Protein Structure, Receptors, Reverse Transcriptase Polymerase Chain Reaction, RNA, Signal Transducing, Tertiary, Toll-Like Receptors, Zygote
@article{kambris_dmmyd88_2003,
title = {DmMyD88 controls dorsoventral patterning of the Drosophila embryo},
author = {Zakaria Kambris and Hana Bilak and Rosalba D'Alessandro and Marcia Belvin and Jean-Luc Imler and Maria Capovilla},
doi = {10.1038/sj.embor.embor714},
issn = {1469-221X},
year = {2003},
date = {2003-01-01},
journal = {EMBO reports},
volume = {4},
number = {1},
pages = {64--69},
abstract = {MyD88 is an adapter protein in the signal transduction pathway mediated by interleukin-1 (IL-1) and Toll-like receptors. A Drosophila homologue of MyD88 (DmMyD88) was recently shown to be required for the Toll-mediated immune response. In Drosophila, the Toll pathway was originally characterized for its role in the dorsoventral patterning of the embryo. We found that, like Toll, DmMyD88 messenger RNA is maternally supplied to the embryo. Here we report the identification of a new mutant allele of DmMyD88, which generates a protein lacking the carboxy-terminal extension, normally located downstream of the Toll/IL-1 receptor domain. Homozygous mutant female flies lay dorsalized embryos that are rescued by expression of a transgenic DmMyD88 complementary DNA. The DmMyD88 mutation blocks the ventralizing activity of a gain-of-function Toll mutation. These results show that DmMyD88 encodes an essential component of the Toll pathway in dorsoventral pattern formation.},
keywords = {Adaptor Proteins, Alleles, Animals, Antigens, Base Sequence, Cell Surface, Complementary, Developmental, Differentiation, DNA, DNA Transposable Elements, Egg Proteins, Embryo, Exons, Female, Gene Expression Regulation, Genetically Modified, Genotype, imler, Immunity, Immunologic, Innate, Insertional, M3i, Male, messenger, Morphogenesis, Mutagenesis, Myeloid Differentiation Factor 88, Nonmammalian, Oocytes, Protein Biosynthesis, Protein Structure, Receptors, Reverse Transcriptase Polymerase Chain Reaction, RNA, Signal Transducing, Tertiary, Toll-Like Receptors, Zygote},
pubstate = {published},
tppubtype = {article}
}
2002
Christophides George K, Zdobnov Evgeny, Barillas-Mury Carolina, Birney Ewan, Blandin Stephanie A, Blass Claudia, Brey Paul T, Collins Frank H, Danielli Alberto, Dimopoulos George, Hetru Charles, Hoa Ngo T, Hoffmann Jules A, Kanzok Stefan M, Letunic Ivica, Levashina Elena A, Loukeris Thanasis G, Lycett Gareth, Meister Stephan, Michel Kristin, Moita Luis F, Müller Hans-Michael, Osta Mike A, Paskewitz Susan M, Reichhart Jean-Marc, Rzhetsky Andrey, Troxler Laurent, Vernick Kenneth D, Vlachou Dina, Volz Jennifer, von Mering Christian, Xu Jiannong, Zheng Liangbiao, Bork Peer, Kafatos Fotis C
Immunity-related genes and gene families in Anopheles gambiae Article de journal
Dans: Science, vol. 298, no. 5591, p. 159–165, 2002, ISSN: 1095-9203.
Résumé | Liens | BibTeX | Étiquettes: Alternative Splicing, Animals, Anopheles, Apoptosis, bacteria, bioinformatic, blandin, Catechol Oxidase, Computational Biology, Enzyme Precursors, Gene Expression Regulation, Genes, Genetic, Genome, hoffmann, Immunity, Innate, Insect, Insect Proteins, M3i, Multigene Family, Peptides, Phylogeny, Plasmodium, Protein Structure, reichhart, Selection, Serine Endopeptidases, Serpins, Signal Transduction, Tertiary
@article{christophides_immunity-related_2002,
title = {Immunity-related genes and gene families in Anopheles gambiae},
author = {George K Christophides and Evgeny Zdobnov and Carolina Barillas-Mury and Ewan Birney and Stephanie A Blandin and Claudia Blass and Paul T Brey and Frank H Collins and Alberto Danielli and George Dimopoulos and Charles Hetru and Ngo T Hoa and Jules A Hoffmann and Stefan M Kanzok and Ivica Letunic and Elena A Levashina and Thanasis G Loukeris and Gareth Lycett and Stephan Meister and Kristin Michel and Luis F Moita and Hans-Michael Müller and Mike A Osta and Susan M Paskewitz and Jean-Marc Reichhart and Andrey Rzhetsky and Laurent Troxler and Kenneth D Vernick and Dina Vlachou and Jennifer Volz and Christian von Mering and Jiannong Xu and Liangbiao Zheng and Peer Bork and Fotis C Kafatos},
url = {http://www.ncbi.nlm.nih.gov/pubmed/12364793},
doi = {10.1126/science.1077136},
issn = {1095-9203},
year = {2002},
date = {2002-10-01},
journal = {Science},
volume = {298},
number = {5591},
pages = {159--165},
abstract = {We have identified 242 Anopheles gambiae genes from 18 gene families implicated in innate immunity and have detected marked diversification relative to Drosophila melanogaster. Immune-related gene families involved in recognition, signal modulation, and effector systems show a marked deficit of orthologs and excessive gene expansions, possibly reflecting selection pressures from different pathogens encountered in these insects' very different life-styles. In contrast, the multifunctional Toll signal transduction pathway is substantially conserved, presumably because of counterselection for developmental stability. Representative expression profiles confirm that sequence diversification is accompanied by specific responses to different immune challenges. Alternative RNA splicing may also contribute to expansion of the immune repertoire.},
keywords = {Alternative Splicing, Animals, Anopheles, Apoptosis, bacteria, bioinformatic, blandin, Catechol Oxidase, Computational Biology, Enzyme Precursors, Gene Expression Regulation, Genes, Genetic, Genome, hoffmann, Immunity, Innate, Insect, Insect Proteins, M3i, Multigene Family, Peptides, Phylogeny, Plasmodium, Protein Structure, reichhart, Selection, Serine Endopeptidases, Serpins, Signal Transduction, Tertiary},
pubstate = {published},
tppubtype = {article}
}
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
Dans: Science, vol. 297, no. 5578, p. 114–116, 2002, ISSN: 1095-9203.
Résumé | Liens | BibTeX | Étiquettes: Animals, Cell Surface, Chromosome Mapping, Escherichia coli, Female, Gene Expression Regulation, Genes, Gram-Positive Cocci, Hemolymph, hoffmann, Hypocreales, Insect, Insect Proteins, M3i, Male, Mutation, Protein Sorting Signals, Protein Structure, Receptors, reichhart, 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 = {Animals, Cell Surface, Chromosome Mapping, Escherichia coli, Female, Gene Expression Regulation, Genes, Gram-Positive Cocci, Hemolymph, hoffmann, Hypocreales, Insect, Insect Proteins, M3i, Male, Mutation, Protein Sorting Signals, Protein Structure, Receptors, reichhart, Serine Endopeptidases, Tertiary, Toll-Like Receptors},
pubstate = {published},
tppubtype = {article}
}
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
Dans: Nature Immunology, vol. 3, no. 1, p. 91–97, 2002, ISSN: 1529-2908.
Résumé | Liens | BibTeX | Étiquettes: Adaptor Proteins, Amino Acid, Animals, 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, hoffmann, Hypocreales, imler, Immunologic, Insect, Insect Proteins, M3i, 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, Animals, 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, hoffmann, Hypocreales, imler, Immunologic, Insect, Insect Proteins, M3i, 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}
}
2001
Georgel Philippe, Naitza S, Kappler Christine, Ferrandon Dominique, Zachary Daniel, Swimmer C, Kopczynski C, Duyk G, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis Article de journal
Dans: Dev. Cell, vol. 1, no. 4, p. 503–514, 2001, ISSN: 1534-5807.
Résumé | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary
@article{georgel_drosophila_2001,
title = {Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis},
author = {Philippe Georgel and S Naitza and Christine Kappler and Dominique Ferrandon and Daniel Zachary and C Swimmer and C Kopczynski and G Duyk and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {1534-5807},
year = {2001},
date = {2001-10-01},
journal = {Dev. Cell},
volume = {1},
number = {4},
pages = {503--514},
abstract = {We report the molecular characterization of the immune deficiency (imd) gene, which controls antibacterial defense in Drosophila. imd encodes a protein with a death domain similar to that of mammalian RIP (receptor interacting protein), a protein that plays a role in both NF-kappaB activation and apoptosis. We show that imd functions upstream of the DmIKK signalosome and the caspase DREDD in the control of antibacterial peptide genes. Strikingly, overexpression of imd leads to constitutive transcription of these genes and to apoptosis, and both effects are blocked by coexpression of the caspase inhibitor P35. We also show that imd is involved in the apoptotic response to UV irradiation. These data raise the possibility that antibacterial response and apoptosis share common control elements in Drosophila.},
keywords = {Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary},
pubstate = {published},
tppubtype = {article}
}
Moine H., Mandel J. L.
Biomedicine. Do G quartets orchestrate fragile X pathology? Article de journal
Dans: Science, vol. 294, no. 5551, p. 2487-8, 2001, (0036-8075 Journal Article).
BibTeX | Étiquettes: Acid, Analysis, Animals, Array, Binding, Brain/metabolism, Conformation, Crystallography, Expression, Fragile, Gene, Genetic, Human, Messenger/*chemistry/genetics/*metabolism, Mice, Nerve, Nucleic, Oligonucleotide, Protein, Proteins/chemistry/genetics/*metabolism, Regions, Regulation, RNA, Sequence, Sites, structure, Synapses/physiology, Syndrome/genetics/*metabolism, Tertiary, Tissue, Translation, Untranslated, X, X-Ray
@article{,
title = {Biomedicine. Do G quartets orchestrate fragile X pathology?},
author = { H. Moine and J. L. Mandel},
year = {2001},
date = {2001-01-01},
journal = {Science},
volume = {294},
number = {5551},
pages = {2487-8},
note = {0036-8075
Journal Article},
keywords = {Acid, Analysis, Animals, Array, Binding, Brain/metabolism, Conformation, Crystallography, Expression, Fragile, Gene, Genetic, Human, Messenger/*chemistry/genetics/*metabolism, Mice, Nerve, Nucleic, Oligonucleotide, Protein, Proteins/chemistry/genetics/*metabolism, Regions, Regulation, RNA, Sequence, Sites, structure, Synapses/physiology, Syndrome/genetics/*metabolism, Tertiary, Tissue, Translation, Untranslated, X, X-Ray},
pubstate = {published},
tppubtype = {article}
}
Levashina Elena A, Moita L F, Blandin Stéphanie A, Vriend G, Lagueux Marie, Kafatos F C
Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae Article de journal
Dans: Cell, vol. 104, no. 5, p. 709–718, 2001, ISSN: 0092-8674.
Résumé | BibTeX | Étiquettes: alpha-Macroglobulins, Animals, Anopheles, blandin, Cells, Cloning, Complement C3, Cultured, DNA Fragmentation, Double-Stranded, Female, Genetic, Gram-Negative Bacteria, Hemocytes, Insect Proteins, M3i, Molecular, Nucleic Acid Denaturation, Phagocytosis, Protein Structure, RNA, Tertiary, Transcription
@article{levashina_conserved_2001,
title = {Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae},
author = {Elena A Levashina and L F Moita and Stéphanie A Blandin and G Vriend and Marie Lagueux and F C Kafatos},
issn = {0092-8674},
year = {2001},
date = {2001-01-01},
journal = {Cell},
volume = {104},
number = {5},
pages = {709--718},
abstract = {We characterize a novel hemocyte-specific acute phase glycoprotein from the malaria vector, Anopheles gambiae. It shows substantial structural and functional similarities, including the highly conserved thioester motif, to both a central component of mammalian complement system, factor C3, and to a pan-protease inhibitor, alpha2-macroglobulin. Most importantly, this protein serves as a complement-like opsonin and promotes phagocytosis of some Gram-negative bacteria in a mosquito hemocyte-like cell line. Chemical inactivation by methylamine and depletion by double-stranded RNA knockout demonstrate that this function is dependent on the internal thioester bond. This evidence of a complement-like function in a protostome animal adds substantially to the accumulating evidence of a common ancestry of immune defenses in insects and vertebrates.},
keywords = {alpha-Macroglobulins, Animals, Anopheles, blandin, Cells, Cloning, Complement C3, Cultured, DNA Fragmentation, Double-Stranded, Female, Genetic, Gram-Negative Bacteria, Hemocytes, Insect Proteins, M3i, Molecular, Nucleic Acid Denaturation, Phagocytosis, Protein Structure, RNA, Tertiary, Transcription},
pubstate = {published},
tppubtype = {article}
}
2000
Imler Jean-Luc, Hoffmann Jules A
Toll and Toll-like proteins: an ancient family of receptors signaling infection Article de journal
Dans: Reviews in Immunogenetics, vol. 2, no. 3, p. 294–304, 2000, ISSN: 1398-1714.
Résumé | BibTeX | Étiquettes: Adaptor Proteins, Animals, Antigens, Autoantigens, CD14, Cell Adhesion Molecules, Cell Surface, Differentiation, DNA-Binding Proteins, Gene Expression Regulation, hoffmann, I-kappa B Proteins, imler, Immunity, Immunologic, infection, Innate, Insect Proteins, Interleukin-1 Receptor-Associated Kinases, Knockout, Larva, Lipopolysaccharides, M3i, Mammals, MAP Kinase Signaling System, Membrane Glycoproteins, Membrane Proteins, Mice, Multigene Family, Myeloid Differentiation Factor 88, NF-kappa B, peptidoglycan, Phosphorylation, Post-Translational, Protein Kinases, Protein Processing, Protein Structure, Receptors, Recombinant Fusion Proteins, Signal Transducing, Signal Transduction, Teichoic Acids, Tertiary, Toll-Like Receptor 4, Toll-Like Receptor 5, Toll-Like Receptor 6, Toll-Like Receptor 9, Toll-Like Receptors, Ubiquitins
@article{imler_toll_2000,
title = {Toll and Toll-like proteins: an ancient family of receptors signaling infection},
author = {Jean-Luc Imler and Jules A Hoffmann},
issn = {1398-1714},
year = {2000},
date = {2000-01-01},
journal = {Reviews in Immunogenetics},
volume = {2},
number = {3},
pages = {294--304},
abstract = {Innate immunity is the first-line host defense of multicellular organisms that rapidly operates to limit infection upon exposure to microbes. It involves intracellular signaling pathways in the fruit-fly Drosophila and in mammals that show striking similarities. Recent genetic and biochemical data have revealed, in particular, that proteins of the Toll family play a critical role in the immediate response to infection. We review here the recent developments on the structural and functional characterization of this evolutionary ancient and important family of proteins, which can function as cytokine receptors (Toll in Drosophila) or pattern recognition receptors (TLR4 in mammals) and activate similar, albeit non identical signal transduction pathways, in flies and mammals.},
keywords = {Adaptor Proteins, Animals, Antigens, Autoantigens, CD14, Cell Adhesion Molecules, Cell Surface, Differentiation, DNA-Binding Proteins, Gene Expression Regulation, hoffmann, I-kappa B Proteins, imler, Immunity, Immunologic, infection, Innate, Insect Proteins, Interleukin-1 Receptor-Associated Kinases, Knockout, Larva, Lipopolysaccharides, M3i, Mammals, MAP Kinase Signaling System, Membrane Glycoproteins, Membrane Proteins, Mice, Multigene Family, Myeloid Differentiation Factor 88, NF-kappa B, peptidoglycan, Phosphorylation, Post-Translational, Protein Kinases, Protein Processing, Protein Structure, Receptors, Recombinant Fusion Proteins, Signal Transducing, Signal Transduction, Teichoic Acids, Tertiary, Toll-Like Receptor 4, Toll-Like Receptor 5, Toll-Like Receptor 6, Toll-Like Receptor 9, Toll-Like Receptors, Ubiquitins},
pubstate = {published},
tppubtype = {article}
}