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2013 |
Petrillo, Jessica E; Venter, Arno P; Short, James R; Gopal, Radhika; Deddouche, Safia; Lamiable, Olivier; Imler, Jean-Luc; Schneemann, Anette Cytoplasmic granule formation and translational inhibition of nodaviral RNAs in the absence of the double-stranded RNA binding protein B2 Article de journal Journal of Virology, 87 (24), p. 13409–13421, 2013, ISSN: 1098-5514. Résumé | Liens | BibTeX | Étiquettes: Animals, Capsid Proteins, Cell Line, Cricetinae, Cytoplasmic Granules, Double-Stranded, imler, M3i, Nodaviridae, Protein Biosynthesis, RNA, RNA Virus Infections, RNA-Binding Proteins, Viral, Viral Proteins @article{petrillo_cytoplasmic_2013, title = {Cytoplasmic granule formation and translational inhibition of nodaviral RNAs in the absence of the double-stranded RNA binding protein B2}, author = {Jessica E Petrillo and Arno P Venter and James R Short and Radhika Gopal and Safia Deddouche and Olivier Lamiable and Jean-Luc Imler and Anette Schneemann}, doi = {10.1128/JVI.02362-13}, issn = {1098-5514}, year = {2013}, date = {2013-12-01}, journal = {Journal of Virology}, volume = {87}, number = {24}, pages = {13409--13421}, abstract = {Flock House virus (FHV) is a positive-sense RNA insect virus with a bipartite genome. RNA1 encodes the RNA-dependent RNA polymerase, and RNA2 encodes the capsid protein. A third protein, B2, is translated from a subgenomic RNA3 derived from the 3' end of RNA1. B2 is a double-stranded RNA (dsRNA) binding protein that inhibits RNA silencing, a major antiviral defense pathway in insects. FHV is conveniently propagated in Drosophila melanogaster cells but can also be grown in mammalian cells. It was previously reported that B2 is dispensable for FHV RNA replication in BHK21 cells; therefore, we chose this cell line to generate a viral mutant that lacked the ability to produce B2. Consistent with published results, we found that RNA replication was indeed vigorous but the yield of progeny virus was negligible. Closer inspection revealed that infected cells contained very small amounts of coat protein despite an abundance of RNA2. B2 mutants that had reduced affinity for dsRNA produced analogous results, suggesting that the dsRNA binding capacity of B2 somehow played a role in coat protein synthesis. Using fluorescence in situ hybridization of FHV RNAs, we discovered that RNA2 is recruited into large cytoplasmic granules in the absence of B2, whereas the distribution of RNA1 remains largely unaffected. We conclude that B2, by binding to double-stranded regions in progeny RNA2, prevents recruitment of RNA2 into cellular structures, where it is translationally silenced. This represents a novel function of B2 that further contributes to successful completion of the nodaviral life cycle.}, keywords = {Animals, Capsid Proteins, Cell Line, Cricetinae, Cytoplasmic Granules, Double-Stranded, imler, M3i, Nodaviridae, Protein Biosynthesis, RNA, RNA Virus Infections, RNA-Binding Proteins, Viral, Viral Proteins}, pubstate = {published}, tppubtype = {article} } Flock House virus (FHV) is a positive-sense RNA insect virus with a bipartite genome. RNA1 encodes the RNA-dependent RNA polymerase, and RNA2 encodes the capsid protein. A third protein, B2, is translated from a subgenomic RNA3 derived from the 3' end of RNA1. B2 is a double-stranded RNA (dsRNA) binding protein that inhibits RNA silencing, a major antiviral defense pathway in insects. FHV is conveniently propagated in Drosophila melanogaster cells but can also be grown in mammalian cells. It was previously reported that B2 is dispensable for FHV RNA replication in BHK21 cells; therefore, we chose this cell line to generate a viral mutant that lacked the ability to produce B2. Consistent with published results, we found that RNA replication was indeed vigorous but the yield of progeny virus was negligible. Closer inspection revealed that infected cells contained very small amounts of coat protein despite an abundance of RNA2. B2 mutants that had reduced affinity for dsRNA produced analogous results, suggesting that the dsRNA binding capacity of B2 somehow played a role in coat protein synthesis. Using fluorescence in situ hybridization of FHV RNAs, we discovered that RNA2 is recruited into large cytoplasmic granules in the absence of B2, whereas the distribution of RNA1 remains largely unaffected. We conclude that B2, by binding to double-stranded regions in progeny RNA2, prevents recruitment of RNA2 into cellular structures, where it is translationally silenced. This represents a novel function of B2 that further contributes to successful completion of the nodaviral life cycle. |
2003 |
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 EMBO reports, 4 (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} } 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. |
1994 |
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, Animals, Antifungal Agents, Base Sequence, Cloning, Complementary, DNA, hoffmann, Insect Proteins, M3i, 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, Animals, Antifungal Agents, Base Sequence, Cloning, Complementary, DNA, hoffmann, Insect Proteins, M3i, 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. |
1974 |
Hoffmann, Jules A; Weins, M J Active protein synthesis in the prothoracic glands and ecdysone titer in the permanent larvae of Locusta migratoria after selective irradiation of hematopoietic tissue Article de journal Experientia, 30 (7), p. 821–822, 1974, ISSN: 0014-4754. BibTeX | Étiquettes: Animals, Ecdysone, Grasshoppers, Hematopoietic System, hoffmann, Larva, Leucine, M3i, Protein Biosynthesis, Radiation Effects, Tritium @article{hoffmann_active_1974, title = {Active protein synthesis in the prothoracic glands and ecdysone titer in the permanent larvae of Locusta migratoria after selective irradiation of hematopoietic tissue}, author = {Jules A Hoffmann and M J Weins}, issn = {0014-4754}, year = {1974}, date = {1974-07-01}, journal = {Experientia}, volume = {30}, number = {7}, pages = {821--822}, keywords = {Animals, Ecdysone, Grasshoppers, Hematopoietic System, hoffmann, Larva, Leucine, M3i, Protein Biosynthesis, Radiation Effects, Tritium}, pubstate = {published}, tppubtype = {article} } |
Goltzené, F; Hoffmann, Jules A Control of haemolymph protein synthesis and oocyte maturation by the corpora allata in female adults of locusta migratoria (Orthoptera): role of the blood-forming tissue Article de journal Gen. Comp. Endocrinol., 22 (4), p. 489–498, 1974, ISSN: 0016-6480. BibTeX | Étiquettes: Animals, Disc, Electrophoresis, Female, Grasshoppers, Hematopoietic System, Hemolymph, hoffmann, M3i, Ovum, Protein Biosynthesis, Radiation Effects @article{goltzene_control_1974, title = {Control of haemolymph protein synthesis and oocyte maturation by the corpora allata in female adults of locusta migratoria (Orthoptera): role of the blood-forming tissue}, author = {F Goltzené and Jules A Hoffmann}, issn = {0016-6480}, year = {1974}, date = {1974-04-01}, journal = {Gen. Comp. Endocrinol.}, volume = {22}, number = {4}, pages = {489--498}, keywords = {Animals, Disc, Electrophoresis, Female, Grasshoppers, Hematopoietic System, Hemolymph, hoffmann, M3i, Ovum, Protein Biosynthesis, Radiation Effects}, pubstate = {published}, tppubtype = {article} } |