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M3i
Insect Models of Innate Immunity
Publications
2015
Aguiar Eric Roberto Guimarães Rocha, Olmo Roenick Proveti, Paro Simona, Ferreira Flavia Viana, da de Faria Isaque João Silva, Todjro Yaovi Mathias Honore, Lobo Francisco Pereira, Kroon Erna Geessien, Meignin Carine, Gatherer Derek, Imler Jean-Luc, Marques João Trindade
Sequence-independent characterization of viruses based on the pattern of viral small RNAs produced by the host Journal Article
In: Nucleic Acids Research, vol. 43, no. 13, pp. 6191–6206, 2015, ISSN: 1362-4962.
Abstract | Links | BibTeX | Tags: Animals, Contig Mapping, Female, imler, insects, M3i, meignin, Ovary, Plants, RNA, Sequence Analysis, Small Untranslated, Vertebrates, Viral, Viral Tropism, viruses
@article{aguiar_sequence-independent_2015,
title = {Sequence-independent characterization of viruses based on the pattern of viral small RNAs produced by the host},
author = {Eric Roberto Guimarães Rocha Aguiar and Roenick Proveti Olmo and Simona Paro and Flavia Viana Ferreira and Isaque João Silva da de Faria and Yaovi Mathias Honore Todjro and Francisco Pereira Lobo and Erna Geessien Kroon and Carine Meignin and Derek Gatherer and Jean-Luc Imler and João Trindade Marques},
url = {http://nar.oxfordjournals.org/lookup/doi/10.1093/nar/gkv587},
doi = {10.1093/nar/gkv587},
issn = {1362-4962},
year = {2015},
date = {2015-07-01},
journal = {Nucleic Acids Research},
volume = {43},
number = {13},
pages = {6191--6206},
abstract = {Virus surveillance in vector insects is potentially of great benefit to public health. Large-scale sequencing of small and long RNAs has previously been used to detect viruses, but without any formal comparison of different strategies. Furthermore, the identification of viral sequences largely depends on similarity searches against reference databases. Here, we developed a sequence-independent strategy based on virus-derived small RNAs produced by the host response, such as the RNA interference pathway. In insects, we compared sequences of small and long RNAs, demonstrating that viral sequences are enriched in the small RNA fraction. We also noted that the small RNA size profile is a unique signature for each virus and can be used to identify novel viral sequences without known relatives in reference databases. Using this strategy, we characterized six novel viruses in the viromes of laboratory fruit flies and wild populations of two insect vectors: mosquitoes and sandflies. We also show that the small RNA profile could be used to infer viral tropism for ovaries among other aspects of virus biology. Additionally, our results suggest that virus detection utilizing small RNAs can also be applied to vertebrates, although not as efficiently as to plants and insects.},
keywords = {Animals, Contig Mapping, Female, imler, insects, M3i, meignin, Ovary, Plants, RNA, Sequence Analysis, Small Untranslated, Vertebrates, Viral, Viral Tropism, viruses},
pubstate = {published},
tppubtype = {article}
}
Virus surveillance in vector insects is potentially of great benefit to public health. Large-scale sequencing of small and long RNAs has previously been used to detect viruses, but without any formal comparison of different strategies. Furthermore, the identification of viral sequences largely depends on similarity searches against reference databases. Here, we developed a sequence-independent strategy based on virus-derived small RNAs produced by the host response, such as the RNA interference pathway. In insects, we compared sequences of small and long RNAs, demonstrating that viral sequences are enriched in the small RNA fraction. We also noted that the small RNA size profile is a unique signature for each virus and can be used to identify novel viral sequences without known relatives in reference databases. Using this strategy, we characterized six novel viruses in the viromes of laboratory fruit flies and wild populations of two insect vectors: mosquitoes and sandflies. We also show that the small RNA profile could be used to infer viral tropism for ovaries among other aspects of virus biology. Additionally, our results suggest that virus detection utilizing small RNAs can also be applied to vertebrates, although not as efficiently as to plants and insects.
1999
Otten L, Salomone J Y, Helfer A, Schmidt J, Hammann P, Ruffray P De
Sequence and functional analysis of the left-hand part of the Ŧ-region from the nopaline-type Ti plasmid, pTiC58. Journal Article
In: Plant molecular biology, vol. 41, no. 6, pp. 765–776, 1999, ISSN: 0167-4412 0167-4412, (Place: Netherlands).
Abstract | Links | BibTeX | Tags: Agrobacterium tumefaciens/*genetics/pathogenicity, Bacterial/chemistry/*genetics, Bacterial/genetics, Chromosome Mapping, DNA, Gene Deletion, Genes, Genetic Complementation Test, Lycopersicon esculentum/genetics/microbiology, Medicinal/genetics/microbiology, Molecular Sequence Data, Mutation, Phylogeny, Plant Tumors/genetics/microbiology, Plants, Plasmids/chemistry/*genetics, PPSE, Sequence Analysis, Species Specificity, Tobacco/genetics/microbiology, Toxic, Virulence/genetics
@article{otten_sequence_1999,
title = {Sequence and functional analysis of the left-hand part of the Ŧ-region from the nopaline-type Ti plasmid, pTiC58.},
author = {L Otten and J Y Salomone and A Helfer and J Schmidt and P Hammann and P De Ruffray},
doi = {10.1023/a:1006370207379},
issn = {0167-4412 0167-4412},
year = {1999},
date = {1999-12-01},
journal = {Plant molecular biology},
volume = {41},
number = {6},
pages = {765--776},
abstract = {The Agrobacterium tumefaciens nopaline strain C58 transfers a large, 29 kb T-DNA into plant cells during infection. Part of this DNA (the 'common DNA') is also found on the T-DNA of octopine strains, the remaining DNA is nopaline strain-specific. Up to now, only parts of the C58 T-DNA and related T37 T-DNA have been sequenced. We have sequenced the remainder of the nopaline-specific T-DNA (containing genes a to d) and acs to iaaM. Gene c codes for a new unknown T-DNA protein. Gene a is homologous to the agrocinopine synthase gene. Genes b, c', d and e are part of a larger family: they are related to the T-DNA genes 5, rolB, lso and 3'. Genes 5, rolB and lso induce or modify plant growth and have been called T-DNA oncogenes. Our studies show that gene 3' (located on the TR-DNA of octopine strains) is also oncogenic. Although the b-e T-DNA fragment from C58 and its individual genes lack growth-inducing activity, an a-acs deletion mutant was distinctly less virulent on Kalanchoe daigremontiana and showed reduced shoot formation on Kalanchoe tubiflora. Shoot formation could be restored by genes c and c' in co-infection experiments. Contrary to an earlier report, a C58 e gene deletion mutant was fully virulent on all plants tested.},
note = {Place: Netherlands},
keywords = {Agrobacterium tumefaciens/*genetics/pathogenicity, Bacterial/chemistry/*genetics, Bacterial/genetics, Chromosome Mapping, DNA, Gene Deletion, Genes, Genetic Complementation Test, Lycopersicon esculentum/genetics/microbiology, Medicinal/genetics/microbiology, Molecular Sequence Data, Mutation, Phylogeny, Plant Tumors/genetics/microbiology, Plants, Plasmids/chemistry/*genetics, PPSE, Sequence Analysis, Species Specificity, Tobacco/genetics/microbiology, Toxic, Virulence/genetics},
pubstate = {published},
tppubtype = {article}
}
The Agrobacterium tumefaciens nopaline strain C58 transfers a large, 29 kb T-DNA into plant cells during infection. Part of this DNA (the 'common DNA') is also found on the T-DNA of octopine strains, the remaining DNA is nopaline strain-specific. Up to now, only parts of the C58 T-DNA and related T37 T-DNA have been sequenced. We have sequenced the remainder of the nopaline-specific T-DNA (containing genes a to d) and acs to iaaM. Gene c codes for a new unknown T-DNA protein. Gene a is homologous to the agrocinopine synthase gene. Genes b, c', d and e are part of a larger family: they are related to the T-DNA genes 5, rolB, lso and 3'. Genes 5, rolB and lso induce or modify plant growth and have been called T-DNA oncogenes. Our studies show that gene 3' (located on the TR-DNA of octopine strains) is also oncogenic. Although the b-e T-DNA fragment from C58 and its individual genes lack growth-inducing activity, an a-acs deletion mutant was distinctly less virulent on Kalanchoe daigremontiana and showed reduced shoot formation on Kalanchoe tubiflora. Shoot formation could be restored by genes c and c' in co-infection experiments. Contrary to an earlier report, a C58 e gene deletion mutant was fully virulent on all plants tested.
1995
Bulet Philippe, Hegy G, Lambert J, van Dorsselaer Alan, Hoffmann Jules A, Hetru Charles
Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity Journal Article
In: Biochemistry, vol. 34, no. 22, pp. 7394–7400, 1995, ISSN: 0006-2960.
Abstract | BibTeX | Tags: Animals, Anti-Bacterial Agents, Carbohydrate Sequence, Carbohydrates, Diptera, Escherichia coli, Glycopeptides, Hemolymph, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mass Spectrometry, Plants, Trisaccharides
@article{bulet_insect_1995,
title = {Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity},
author = {Philippe Bulet and G Hegy and J Lambert and Alan van Dorsselaer and Jules A Hoffmann and Charles Hetru},
issn = {0006-2960},
year = {1995},
date = {1995-06-01},
journal = {Biochemistry},
volume = {34},
number = {22},
pages = {7394--7400},
abstract = {A bacterial challenge of larvae of the dipteran insect Phormia terranovae induces the rapid synthesis of diptericin, an antibacterial polypeptide, previously characterized at the amino acid level and indirectly by cDNA cloning studies. This 82-residue polypeptide consists of an N-terminal proline-rich domain and a central and C-terminal glycine-rich domain. Using liquid chromatography coupled to electrospray ionization-mass spectrometry, we demonstrate here that this molecule is more complex than anticipated and carries two O-substitutions on threonine residues, one in the proline-rich domain (residue 10) and one in the glycine-rich domain (residue 54). These substitutions consist of identical trisaccharides: glucose--textgreatergalactose--textgreaterN-acetylgalactosamine--textgreater(threonine). Treatment of diptericin with O-glycosidase, which selectively removes the substitutions without altering the polypeptide proper, abolishes the antibacterial activity, indicating that this posttranslational modification is essential for biological activity of the polypeptide. We also show that diptericin is posttranslationally modified by a C-terminal amidation.},
keywords = {Animals, Anti-Bacterial Agents, Carbohydrate Sequence, Carbohydrates, Diptera, Escherichia coli, Glycopeptides, Hemolymph, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mass Spectrometry, Plants, Trisaccharides},
pubstate = {published},
tppubtype = {article}
}
A bacterial challenge of larvae of the dipteran insect Phormia terranovae induces the rapid synthesis of diptericin, an antibacterial polypeptide, previously characterized at the amino acid level and indirectly by cDNA cloning studies. This 82-residue polypeptide consists of an N-terminal proline-rich domain and a central and C-terminal glycine-rich domain. Using liquid chromatography coupled to electrospray ionization-mass spectrometry, we demonstrate here that this molecule is more complex than anticipated and carries two O-substitutions on threonine residues, one in the proline-rich domain (residue 10) and one in the glycine-rich domain (residue 54). These substitutions consist of identical trisaccharides: glucose--textgreatergalactose--textgreaterN-acetylgalactosamine--textgreater(threonine). Treatment of diptericin with O-glycosidase, which selectively removes the substitutions without altering the polypeptide proper, abolishes the antibacterial activity, indicating that this posttranslational modification is essential for biological activity of the polypeptide. We also show that diptericin is posttranslationally modified by a C-terminal amidation.
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 Journal Article
In: J. Biol. Chem., vol. 269, no. 52, pp. 33159–33163, 1994, ISSN: 0021-9258.
Abstract | BibTeX | Tags: 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.
1973
Koolman J, Hoffmann Jules A, Karlson P
Sulphage esters as inactivation products of ecdysone in Locusta migratoria Journal Article
In: Hoppe-Seyler's Z. Physiol. Chem., vol. 354, no. 9, pp. 1043–1048, 1973, ISSN: 0018-4888.
BibTeX | Tags: Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium
@article{koolman_sulphage_1973,
title = {Sulphage esters as inactivation products of ecdysone in Locusta migratoria},
author = {J Koolman and Jules A Hoffmann and P Karlson},
issn = {0018-4888},
year = {1973},
date = {1973-09-01},
journal = {Hoppe-Seyler's Z. Physiol. Chem.},
volume = {354},
number = {9},
pages = {1043--1048},
keywords = {Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium},
pubstate = {published},
tppubtype = {article}
}