Publications
2014 |
|
Articles de journaux |
|
| 9. | Schwarzmüller, Tobias; Ma, Biao; Hiller, Ekkehard; Istel, Fabian; Tscherner, Michael; Brunke, Sascha; Ames, Lauren; Firon, Arnaud; Green, Brian; Cabral, Vitor; Marcet-Houben, Marina; Jacobsen, Ilse D; Quintin, Jessica; Seider, Katja; Frohner, Ingrid; Glaser, Walter; Jungwirth, Helmut; Bachellier-Bassi, Sophie; Chauvel, Murielle; Zeidler, Ute; Ferrandon, Dominique; Gabaldón, Toni; Hube, Bernhard; d'Enfert, Christophe; Rupp, Steffen; Cormack, Brendan; Haynes, Ken; Kuchler, Karl Systematic phenotyping of a large-scale Candida glabrata deletion collection reveals novel antifungal tolerance genes Article de journal PLoS Pathog., 10 (6), p. e1004211, 2014, ISSN: 1553-7374. Résumé | Liens | BibTeX | Étiquettes: Antifungal Agents, Azoles, Biofilms, Candida glabrata, Candidiasis, Cell Wall, Drug Resistance, Echinocandins, Fungal, Fungal Proteins, Gene Deletion, Gene Knockout Techniques, Gene Library, Microbial Sensitivity Tests, Osmotic Pressure, Phenotype @article{schwarzmuller_systematic_2014b, title = {Systematic phenotyping of a large-scale Candida glabrata deletion collection reveals novel antifungal tolerance genes}, author = { Tobias Schwarzmüller and Biao Ma and Ekkehard Hiller and Fabian Istel and Michael Tscherner and Sascha Brunke and Lauren Ames and Arnaud Firon and Brian Green and Vitor Cabral and Marina Marcet-Houben and Ilse D. Jacobsen and Jessica Quintin and Katja Seider and Ingrid Frohner and Walter Glaser and Helmut Jungwirth and Sophie Bachellier-Bassi and Murielle Chauvel and Ute Zeidler and Dominique Ferrandon and Toni Gabaldón and Bernhard Hube and Christophe d'Enfert and Steffen Rupp and Brendan Cormack and Ken Haynes and Karl Kuchler}, doi = {10.1371/journal.ppat.1004211}, issn = {1553-7374}, year = {2014}, date = {2014-01-01}, journal = {PLoS Pathog.}, volume = {10}, number = {6}, pages = {e1004211}, abstract = {The opportunistic fungal pathogen Candida glabrata is a frequent cause of candidiasis, causing infections ranging from superficial to life-threatening disseminated disease. The inherent tolerance of C. glabrata to azole drugs makes this pathogen a serious clinical threat. To identify novel genes implicated in antifungal drug tolerance, we have constructed a large-scale C. glabrata deletion library consisting of 619 unique, individually bar-coded mutant strains, each lacking one specific gene, all together representing almost 12% of the genome. Functional analysis of this library in a series of phenotypic and fitness assays identified numerous genes required for growth of C. glabrata under normal or specific stress conditions, as well as a number of novel genes involved in tolerance to clinically important antifungal drugs such as azoles and echinocandins. We identified 38 deletion strains displaying strongly increased susceptibility to caspofungin, 28 of which encoding proteins that have not previously been linked to echinocandin tolerance. Our results demonstrate the potential of the C. glabrata mutant collection as a valuable resource in functional genomics studies of this important fungal pathogen of humans, and to facilitate the identification of putative novel antifungal drug target and virulence genes.}, keywords = {Antifungal Agents, Azoles, Biofilms, Candida glabrata, Candidiasis, Cell Wall, Drug Resistance, Echinocandins, Fungal, Fungal Proteins, Gene Deletion, Gene Knockout Techniques, Gene Library, Microbial Sensitivity Tests, Osmotic Pressure, Phenotype}, pubstate = {published}, tppubtype = {article} } The opportunistic fungal pathogen Candida glabrata is a frequent cause of candidiasis, causing infections ranging from superficial to life-threatening disseminated disease. The inherent tolerance of C. glabrata to azole drugs makes this pathogen a serious clinical threat. To identify novel genes implicated in antifungal drug tolerance, we have constructed a large-scale C. glabrata deletion library consisting of 619 unique, individually bar-coded mutant strains, each lacking one specific gene, all together representing almost 12% of the genome. Functional analysis of this library in a series of phenotypic and fitness assays identified numerous genes required for growth of C. glabrata under normal or specific stress conditions, as well as a number of novel genes involved in tolerance to clinically important antifungal drugs such as azoles and echinocandins. We identified 38 deletion strains displaying strongly increased susceptibility to caspofungin, 28 of which encoding proteins that have not previously been linked to echinocandin tolerance. Our results demonstrate the potential of the C. glabrata mutant collection as a valuable resource in functional genomics studies of this important fungal pathogen of humans, and to facilitate the identification of putative novel antifungal drug target and virulence genes. |
2012 |
|
Articles de journaux |
|
| 8. | Lemaitre, Bruno; Nicolas, Emmanuelle ; Michaut, Lydia ; Reichhart, Jean-Marc ; Hoffmann, Jules A Pillars article: the dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell. 1996. 86: 973-983 Article de journal J. Immunol., 188 (11), p. 5210–5220, 2012, ISSN: 1550-6606. Résumé | BibTeX | Étiquettes: Antifungal Agents, Developmental, DNA-Binding Proteins, Gene Expression Regulation, History, Multigene Family, Mycoses, Phosphoproteins, Toll-Like Receptors @article{lemaitre_pillars_2012, title = {Pillars article: the dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell. 1996. 86: 973-983}, author = { Bruno Lemaitre and Emmanuelle Nicolas and Lydia Michaut and Jean-Marc Reichhart and Jules A. Hoffmann}, issn = {1550-6606}, year = {2012}, date = {2012-06-01}, journal = {J. Immunol.}, volume = {188}, number = {11}, pages = {5210--5220}, abstract = {The cytokine-induced activation cascade of NF-kappaB in mammals and the activation of the morphogen dorsal in Drosophila embryos show striking structural and functional similarities (Toll/IL-1, Cactus/I-kappaB, and dorsal/NF-kappaB). Here we demonstrate that these parallels extend to the immune response of Drosophila. In particular, the intracellular components of the dorsoventral signaling pathway (except for dorsal) and the extracellular Toll ligand, spätzle regulatory gene cassette, control expression of the antifungal peptide gene drosomycin in adults. We also show that mutations in the Toll signaling pathway dramatically reduce survival after fungal infection. Antibacterial genes are induced either by a distinct pathway involving the immune deficiency gene (imd) or by combined activation of both imd and dorsoventral pathways.}, keywords = {Antifungal Agents, Developmental, DNA-Binding Proteins, Gene Expression Regulation, History, Multigene Family, Mycoses, Phosphoproteins, Toll-Like Receptors}, pubstate = {published}, tppubtype = {article} } The cytokine-induced activation cascade of NF-kappaB in mammals and the activation of the morphogen dorsal in Drosophila embryos show striking structural and functional similarities (Toll/IL-1, Cactus/I-kappaB, and dorsal/NF-kappaB). Here we demonstrate that these parallels extend to the immune response of Drosophila. In particular, the intracellular components of the dorsoventral signaling pathway (except for dorsal) and the extracellular Toll ligand, spätzle regulatory gene cassette, control expression of the antifungal peptide gene drosomycin in adults. We also show that mutations in the Toll signaling pathway dramatically reduce survival after fungal infection. Antibacterial genes are induced either by a distinct pathway involving the immune deficiency gene (imd) or by combined activation of both imd and dorsoventral pathways. |
2001 |
|
Articles de journaux |
|
| 7. | Lamberty, M; Zachary, Daniel; Lanot, R; Bordereau, C; Robert, A; Hoffmann, Jules A; Bulet, Philippe Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect. Article de journal J. Biol. Chem., 276 (6), p. 4085–4092, 2001, ISSN: 0021-9258. Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Anti-Bacterial Agents, Antifungal Agents, Base Sequence, Chromatography, Cysteine, DNA Primers, High Pressure Liquid, Immunohistochemistry, Isoptera, Peptides, Protein Conformation, Recombinant Proteins, Sequence Homology @article{lamberty_insect_2001, title = {Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect.}, author = { M. Lamberty and Daniel Zachary and R. Lanot and C. Bordereau and A. Robert and Jules A. Hoffmann and Philippe Bulet}, doi = {10.1074/jbc.M002998200}, issn = {0021-9258}, year = {2001}, date = {2001-02-01}, journal = {J. Biol. Chem.}, volume = {276}, number = {6}, pages = {4085--4092}, abstract = {Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively present in hemocyte granules and in salivary glands. The presence of termicin and spinigerin in unchallenged termites contrasts with observations in evolutionary recent insects or insects undergoing complete metamorphosis, in which antimicrobial peptides are induced in the fat body and released into the hemolymph after septic injury.}, keywords = {Amino Acid, Anti-Bacterial Agents, Antifungal Agents, Base Sequence, Chromatography, Cysteine, DNA Primers, High Pressure Liquid, Immunohistochemistry, Isoptera, Peptides, Protein Conformation, Recombinant Proteins, Sequence Homology}, pubstate = {published}, tppubtype = {article} } Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively present in hemocyte granules and in salivary glands. The presence of termicin and spinigerin in unchallenged termites contrasts with observations in evolutionary recent insects or insects undergoing complete metamorphosis, in which antimicrobial peptides are induced in the fat body and released into the hemolymph after septic injury. |
1999 |
|
Articles de journaux |
|
| 6. | Levashina, Elena A; Langley, E; Green, C; Gubb, David ; Ashburner, M; Hoffmann, Jules A; Reichhart, Jean-Marc Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila Article de journal Science, 285 (5435), p. 1917–1919, 1999, ISSN: 0036-8075. Résumé | BibTeX | Étiquettes: Antifungal Agents, Antimicrobial Cationic Peptides, Body Patterning, Cell Surface, Escherichia coli, Genes, Hemolymph, Insect, Insect Proteins, Membrane Glycoproteins, Micrococcus luteus, Mutagenesis, Peptides, Receptors, Recombinant Fusion Proteins, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors, Up-Regulation @article{levashina_constitutive_1999, title = {Constitutive activation of toll-mediated antifungal defense in serpin-deficient Drosophila}, author = { Elena A. Levashina and E. Langley and C. Green and David Gubb and M. Ashburner and Jules A. Hoffmann and Jean-Marc Reichhart}, issn = {0036-8075}, year = {1999}, date = {1999-09-01}, journal = {Science}, volume = {285}, number = {5435}, pages = {1917--1919}, abstract = {The antifungal defense of Drosophila is controlled by the spaetzle/Toll/cactus gene cassette. Here, a loss-of-function mutation in the gene encoding a blood serine protease inhibitor, Spn43Ac, was shown to lead to constitutive expression of the antifungal peptide drosomycin, and this effect was mediated by the spaetzle and Toll gene products. Spaetzle was cleaved by proteolytic enzymes to its active ligand form shortly after immune challenge, and cleaved Spaetzle was constitutively present in Spn43Ac-deficient flies. Hence, Spn43Ac negatively regulates the Toll signaling pathway, and Toll does not function as a pattern recognition receptor in the Drosophila host defense.}, keywords = {Antifungal Agents, Antimicrobial Cationic Peptides, Body Patterning, Cell Surface, Escherichia coli, Genes, Hemolymph, Insect, Insect Proteins, Membrane Glycoproteins, Micrococcus luteus, Mutagenesis, Peptides, Receptors, Recombinant Fusion Proteins, Serine Proteinase Inhibitors, Serpins, Signal Transduction, Toll-Like Receptors, Up-Regulation}, pubstate = {published}, tppubtype = {article} } The antifungal defense of Drosophila is controlled by the spaetzle/Toll/cactus gene cassette. Here, a loss-of-function mutation in the gene encoding a blood serine protease inhibitor, Spn43Ac, was shown to lead to constitutive expression of the antifungal peptide drosomycin, and this effect was mediated by the spaetzle and Toll gene products. Spaetzle was cleaved by proteolytic enzymes to its active ligand form shortly after immune challenge, and cleaved Spaetzle was constitutively present in Spn43Ac-deficient flies. Hence, Spn43Ac negatively regulates the Toll signaling pathway, and Toll does not function as a pattern recognition receptor in the Drosophila host defense. |
| 5. | Lamberty, M; Ades, S; Uttenweiler-Joseph, S; Brookhart, G; Bushey, D; Hoffmann, Jules A; Bulet, Philippe Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity Article de journal J. Biol. Chem., 274 (14), p. 9320–9326, 1999, ISSN: 0021-9258. Résumé | BibTeX | Étiquettes: Amino Acid, Antifungal Agents, Capillary, Chromatography, Defensins, Electrophoresis, Escherichia coli, Hemolymph, High Pressure Liquid, Insect Proteins, Larva, Lepidoptera, Micrococcus luteus, Proteins, Sequence Homology @article{lamberty_insect_1999, title = {Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity}, author = { M. Lamberty and S. Ades and S. Uttenweiler-Joseph and G. Brookhart and D. Bushey and Jules A. Hoffmann and Philippe Bulet}, issn = {0021-9258}, year = {1999}, date = {1999-04-01}, journal = {J. Biol. Chem.}, volume = {274}, number = {14}, pages = {9320--9326}, abstract = {Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements.}, keywords = {Amino Acid, Antifungal Agents, Capillary, Chromatography, Defensins, Electrophoresis, Escherichia coli, Hemolymph, High Pressure Liquid, Insect Proteins, Larva, Lepidoptera, Micrococcus luteus, Proteins, Sequence Homology}, pubstate = {published}, tppubtype = {article} } Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements. |
1996 |
|
Articles de journaux |
|
| 4. | Charlet, Maurice; Chernysh, S; Philippe, H; Hetru, Charles; Hoffmann, Jules A; Bulet, Philippe Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis Article de journal J. Biol. Chem., 271 (36), p. 21808–21813, 1996, ISSN: 0021-9258. Résumé | BibTeX | Étiquettes: Amino Acid, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, Molecular Weight, Phylogeny, Sequence Homology @article{charlet_innate_1996, title = {Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis}, author = { Maurice Charlet and S. Chernysh and H. Philippe and Charles Hetru and Jules A. Hoffmann and Philippe Bulet}, issn = {0021-9258}, year = {1996}, date = {1996-09-01}, journal = {J. Biol. Chem.}, volume = {271}, number = {36}, pages = {21808--21813}, abstract = {We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.}, keywords = {Amino Acid, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, Molecular Weight, Phylogeny, Sequence Homology}, pubstate = {published}, tppubtype = {article} } We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago. |
| 3. | Lemaitre, Bruno; Nicolas, E; Michaut, Lydia ; Reichhart, Jean-Marc ; Hoffmann, Jules A The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults Article de journal Cell, 86 (6), p. 973–983, 1996, ISSN: 0092-8674. Résumé | BibTeX | Étiquettes: Antifungal Agents, Cell Surface, DNA-Binding Proteins, Fungi, Gene Expression, Genes, Insect, Insect Hormones, Insect Proteins, Membrane Glycoproteins, MHC Class II, Mutation, Mycoses, NF-kappa B, Phosphoproteins, Proteins, Receptors, Signal Transduction, Toll-Like Receptors @article{lemaitre_dorsoventral_1996, title = {The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults}, author = { Bruno Lemaitre and E. Nicolas and Lydia Michaut and Jean-Marc Reichhart and Jules A. Hoffmann}, issn = {0092-8674}, year = {1996}, date = {1996-01-01}, journal = {Cell}, volume = {86}, number = {6}, pages = {973--983}, abstract = {The cytokine-induced activation cascade of NF-kappaB in mammals and the activation of the morphogen dorsal in Drosophila embryos show striking structural and functional similarities (Toll/IL-1, Cactus/I-kappaB, and dorsal/NF-kappaB). Here we demonstrate that these parallels extend to the immune response of Drosophila. In particular, the intracellular components of the dorsoventral signaling pathway (except for dorsal) and the extracellular Toll ligand, spätzle, control expression of the antifungal peptide gene drosomycin in adults. We also show that mutations in the Toll signaling pathway dramatically reduce survival after fungal infection. Antibacterial genes are induced either by a distinct pathway involving the immune deficiency gene (imd) or by combined activation of both imd and dorsoventral pathways.}, keywords = {Antifungal Agents, Cell Surface, DNA-Binding Proteins, Fungi, Gene Expression, Genes, Insect, Insect Hormones, Insect Proteins, Membrane Glycoproteins, MHC Class II, Mutation, Mycoses, NF-kappa B, Phosphoproteins, Proteins, Receptors, Signal Transduction, Toll-Like Receptors}, pubstate = {published}, tppubtype = {article} } The cytokine-induced activation cascade of NF-kappaB in mammals and the activation of the morphogen dorsal in Drosophila embryos show striking structural and functional similarities (Toll/IL-1, Cactus/I-kappaB, and dorsal/NF-kappaB). Here we demonstrate that these parallels extend to the immune response of Drosophila. In particular, the intracellular components of the dorsoventral signaling pathway (except for dorsal) and the extracellular Toll ligand, spätzle, control expression of the antifungal peptide gene drosomycin in adults. We also show that mutations in the Toll signaling pathway dramatically reduce survival after fungal infection. Antibacterial genes are induced either by a distinct pathway involving the immune deficiency gene (imd) or by combined activation of both imd and dorsoventral pathways. |
1995 |
|
Articles de journaux |
|
| 2. | Levashina, Elena A; Ohresser, S; Bulet, Philippe ; Reichhart, Jean-Marc ; Hetru, Charles ; Hoffmann, Jules A Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties Article de journal Eur. J. Biochem., 233 (2), p. 694–700, 1995, ISSN: 0014-2956. Résumé | BibTeX | Étiquettes: Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, Bacteria, Base Sequence, Cells, Chromosome Mapping, Cloning, Cultured, Genetic, Molecular, Peptides, Proline, Transcription @article{levashina_metchnikowin_1995, title = {Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties}, author = { Elena A. Levashina and S. Ohresser and Philippe Bulet and Jean-Marc Reichhart and Charles Hetru and Jules A. Hoffmann}, issn = {0014-2956}, year = {1995}, date = {1995-10-01}, journal = {Eur. J. Biochem.}, volume = {233}, number = {2}, pages = {694--700}, abstract = {One of the characteristics of the host defense of higher insects is the rapid and transient synthesis of a variety of potent antimicrobial peptides. To date, several distinct inducible antimicrobial peptides or peptide families have been totally or partially characterized. We present here the isolation and characterization of a novel 26-residue proline-rich immune-inducible peptide from Drosophila, which exhibits both antibacterial (Gram-positive) and antifungal activities. Peptide sequencing and cDNA cloning indicate the presense of two isoforms in our Drosophila Oregon strain, which differ by one residue (His compared to Arg) as a consequence of a single nucleotide change. The gene, which maps in position 52A1-2 on the right arm of the second chromosome, is expressed in the fat body after immune challenge. The novel peptide, which we propose to name metchnikowin, is a member of a family of proline-rich peptides, and we discuss the possible evolutionary relationships within this family.}, keywords = {Anti-Bacterial Agents, Antifungal Agents, Antimicrobial Cationic Peptides, Bacteria, Base Sequence, Cells, Chromosome Mapping, Cloning, Cultured, Genetic, Molecular, Peptides, Proline, Transcription}, pubstate = {published}, tppubtype = {article} } One of the characteristics of the host defense of higher insects is the rapid and transient synthesis of a variety of potent antimicrobial peptides. To date, several distinct inducible antimicrobial peptides or peptide families have been totally or partially characterized. We present here the isolation and characterization of a novel 26-residue proline-rich immune-inducible peptide from Drosophila, which exhibits both antibacterial (Gram-positive) and antifungal activities. Peptide sequencing and cDNA cloning indicate the presense of two isoforms in our Drosophila Oregon strain, which differ by one residue (His compared to Arg) as a consequence of a single nucleotide change. The gene, which maps in position 52A1-2 on the right arm of the second chromosome, is expressed in the fat body after immune challenge. The novel peptide, which we propose to name metchnikowin, is a member of a family of proline-rich peptides, and we discuss the possible evolutionary relationships within this family. |
1994 |
|
Articles de journaux |
|
| 1. | Fehlbaum, P; Bulet, Philippe; Michaut, L; Lagueux, Marie; Broekaert, W F; Hetru, Charles; Hoffmann, Jules A Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides Article de journal J. Biol. Chem., 269 (52), p. 33159–33163, 1994, ISSN: 0021-9258. Résumé | BibTeX | Étiquettes: Amino Acid, Antifungal Agents, Base Sequence, Cloning, Complementary, DNA, Insect Proteins, Male, Messenger, Microbial Sensitivity Tests, Molecular, Peptide Biosynthesis, Peptides, Plants, Protein Biosynthesis, Protein Precursors, Proteins, RNA, Sequence Homology @article{fehlbaum_insect_1994, title = {Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides}, author = {P. Fehlbaum and Philippe Bulet and L. Michaut and Marie Lagueux and W. F. Broekaert and Charles Hetru and Jules A. Hoffmann}, issn = {0021-9258}, year = {1994}, date = {1994-12-01}, journal = {J. Biol. Chem.}, volume = {269}, number = {52}, pages = {33159--33163}, abstract = {In response to a septic injury (pricking with a bacteria-soaked needle) larvae and adults of Drosophila produce considerable amounts of a 44-residue peptide containing 8 cysteines engaged in intramolecular disulfide bridges. The peptide is synthesized in the fat body, a functional homologue of the mammalian liver, and secreted into the blood of the insect. It exhibits potent antifungal activity but is inactive against bacteria. This novel inducible peptide, which we propose to name drosomycin, shows a significant homology with a family of 5-kDa cysteine-rich plant antifungal peptides recently isolated from seeds of Brassicaceae. This finding underlines that plants and insects can rely on similar molecules in their innate host defense.}, keywords = {Amino Acid, Antifungal Agents, Base Sequence, Cloning, Complementary, DNA, Insect Proteins, Male, Messenger, Microbial Sensitivity Tests, Molecular, Peptide Biosynthesis, Peptides, Plants, Protein Biosynthesis, Protein Precursors, Proteins, RNA, Sequence Homology}, pubstate = {published}, tppubtype = {article} } In response to a septic injury (pricking with a bacteria-soaked needle) larvae and adults of Drosophila produce considerable amounts of a 44-residue peptide containing 8 cysteines engaged in intramolecular disulfide bridges. The peptide is synthesized in the fat body, a functional homologue of the mammalian liver, and secreted into the blood of the insect. It exhibits potent antifungal activity but is inactive against bacteria. This novel inducible peptide, which we propose to name drosomycin, shows a significant homology with a family of 5-kDa cysteine-rich plant antifungal peptides recently isolated from seeds of Brassicaceae. This finding underlines that plants and insects can rely on similar molecules in their innate host defense. |
Partenaires:
Informations générales
Dernières actualités
Adresse
IBMC - UPR9022 CNRS
15 rue René Descartes
67084 STRASBOURG cedex
Tel: (33) 03 88 41 70 37
Fax: (33) 03 88 60 69 22
15 rue René Descartes
67084 STRASBOURG cedex
Tel: (33) 03 88 41 70 37
Fax: (33) 03 88 60 69 22
© M3I – UPR9022 CNRS