Publications
2012
Niehus Sebastian, Giammarinaro Philippe, Liégeois Samuel, Quintin Jessica, Ferrandon Dominique
In: Fly (Austin), vol. 6, no. 3, pp. 193–204, 2012, ISSN: 1933-6942.
Abstract | Links | BibTeX | Tags: Animals, Apansporoblastina, Apansporoblastina/*genetics/physiology, Base Sequence, cure, Disinfection, Disinfection/methods, DNA, DNA Primers, Drosophila melanogaster/*microbiology, ferrandon, fumagillin, Fungal, Fungal/chemistry, M3i, microsporidia, obligate intracellular parasitism, PCR detection, Phylogeny, Polymerase Chain Reaction, Polymerase Chain Reaction/methods, prophylaxis, Ribosomal, Ribosomal/chemistry, Sequence Alignment, Tubulinosema ratisbonensis
@article{niehus_fly_2012b,
title = {Fly culture collapse disorder: detection, prophylaxis and eradication of the microsporidian parasite Tubulinosema ratisbonensis infecting Drosophila melanogaster},
author = {Sebastian Niehus and Philippe Giammarinaro and Samuel Liégeois and Jessica Quintin and Dominique Ferrandon},
doi = {10.4161/fly.20896},
issn = {1933-6942},
year = {2012},
date = {2012-01-01},
journal = {Fly (Austin)},
volume = {6},
number = {3},
pages = {193--204},
abstract = {Drosophila melanogaster is a robust model to investigate many biological problems. It is however prone to some infections, which may endanger fly stocks if left unchecked for. One such infection is caused by an obligate fungal intracellular parasite, Tubulinosema ratisbonensis, which can be found in laboratory stocks. Here, we identify and briefly characterize a T. ratisbonensis strain that was infesting our Drosophila cultures and that required intensive measures to contain and eradicate the infection. We describe the phenotypes of infested stocks. We also report PCR-based techniques that allow the detection of infested stocks with a high sensitivity. We have developed a high-throughput qPCR assay that allows the efficient parallel screening of a large number of potentially-infested stocks. We also have investigated several prophylactic measures to prevent the further contamination of stocks, namely UV-exposure, ethanol treatment, bleaching, and desiccation. Bleaching was found to kill all spores. Other treatments were less effective but were found to be sufficient to prevent further contamination of noninfested stocks. Two treatments were efficacious in curing infested stocks (1) bleaching of eggs and subsequent raising of the larvae in clean vials; (2) fumagillin treatment. These cures only work on stocks that have not become too weak to withstand the procedures.},
keywords = {Animals, Apansporoblastina, Apansporoblastina/*genetics/physiology, Base Sequence, cure, Disinfection, Disinfection/methods, DNA, DNA Primers, Drosophila melanogaster/*microbiology, ferrandon, fumagillin, Fungal, Fungal/chemistry, M3i, microsporidia, obligate intracellular parasitism, PCR detection, Phylogeny, Polymerase Chain Reaction, Polymerase Chain Reaction/methods, prophylaxis, Ribosomal, Ribosomal/chemistry, Sequence Alignment, Tubulinosema ratisbonensis},
pubstate = {published},
tppubtype = {article}
}
2010
den Bossche Jeroen Van, Al-Jamal Wafa' T, Tian Bowen, Nunes Antonio, Fabbro Chiara, Bianco Alberto, Prato Maurizio, Kostarelos Kostas
Efficient receptor-independent intracellular translocation of aptamers mediated by conjugation to carbon nanotubes Journal Article
In: Chemical Communications (Cambridge, England), vol. 46, no. 39, pp. 7379–7381, 2010, ISSN: 1364-548X.
Abstract | Links | BibTeX | Tags: Aptamers, Base Sequence, Biological Transport, carbon, Cell Line, Cell Surface, DNA Primers, Electron, Electrophoresis, Humans, I2CT, Microscopy, Nanotubes, Nucleotide, Polyacrylamide Gel, Receptors, Team-Bianco, Transmission, tumor
@article{van_den_bossche_efficient_2010,
title = {Efficient receptor-independent intracellular translocation of aptamers mediated by conjugation to carbon nanotubes},
author = {Jeroen Van den Bossche and Wafa' T Al-Jamal and Bowen Tian and Antonio Nunes and Chiara Fabbro and Alberto Bianco and Maurizio Prato and Kostas Kostarelos},
doi = {10.1039/c0cc02092c},
issn = {1364-548X},
year = {2010},
date = {2010-10-01},
journal = {Chemical Communications (Cambridge, England)},
volume = {46},
number = {39},
pages = {7379--7381},
abstract = {We have covalently grafted aptamers onto carboxylated carbon nanotubes to design a novel vector system that can easily translocate into the cytosol of different cell types independent of receptor-mediated uptake. We propose the use of carbon nanotubes for the efficient intracellular delivery of biologically active aptamers for potential therapeutic applications.},
keywords = {Aptamers, Base Sequence, Biological Transport, carbon, Cell Line, Cell Surface, DNA Primers, Electron, Electrophoresis, Humans, I2CT, Microscopy, Nanotubes, Nucleotide, Polyacrylamide Gel, Receptors, Team-Bianco, Transmission, tumor},
pubstate = {published},
tppubtype = {article}
}
2001
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. Journal Article
In: J. Biol. Chem., vol. 276, no. 6, pp. 4085–4092, 2001, ISSN: 0021-9258.
Abstract | Links | BibTeX | Tags: Amino Acid, Animals, Anti-Bacterial Agents, Antifungal Agents, Base Sequence, Chromatography, Cysteine, DNA Primers, High Pressure Liquid, hoffmann, Immunohistochemistry, Isoptera, M3i, 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, Animals, Anti-Bacterial Agents, Antifungal Agents, Base Sequence, Chromatography, Cysteine, DNA Primers, High Pressure Liquid, hoffmann, Immunohistochemistry, Isoptera, M3i, Peptides, Protein Conformation, Recombinant Proteins, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
1996
Gross I, Georgel Philippe, Kappler Christine, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin Journal Article
In: Nucleic Acids Res., vol. 24, no. 7, pp. 1238–1245, 1996, ISSN: 0305-1048.
Abstract | BibTeX | Tags: Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation
@article{gross_drosophila_1996,
title = {Drosophila immunity: a comparative analysis of the Rel proteins dorsal and Dif in the induction of the genes encoding diptericin and cecropin},
author = {I Gross and Philippe Georgel and Christine Kappler and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0305-1048},
year = {1996},
date = {1996-04-01},
journal = {Nucleic Acids Res.},
volume = {24},
number = {7},
pages = {1238--1245},
abstract = {In Drosophila, bacterial challenge induces the rapid transcription of several genes encoding potent antibacterial peptides. The upstream sequences of the diptericin and cecropin Al genes, which have been investigated in detail, contain two, respectively one sequence element homologous to the binding site of the mammalian nuclear factor kappaB. These elements have been shown to be mandatory for immune-induced transcription of both genes. Functional studies have shown that these kappaB-related elements can be the target for the Drosophila Rel proteins dorsal and Dif. Here we present a comparative analysis of the transactivating capacities of these proteins on reporter genes fused to either the diptericin or the cecropin kappaB-related motifs. We conclude from our results: (i) the kappaB motifs of the diptericin and cecropin genes are not functionally equivalent; (ii) the dorsal and Dif proteins have distinct DNA-binding characteristics; (iii) dorsal and Dif can heterodimerize in vitro; (iv) mutants containing no copies of dorsal and a single copy of Dif retain their full capacity to express the diptericin and cecropin genes in response to challenge.},
keywords = {Animals, Antimicrobial Cationic Peptides, Base Sequence, DNA Primers, DNA-Binding Proteins, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, NF-kappa B, Nuclear Proteins, Peptides, Phosphoproteins, reichhart, Transcription, Transcription Factors, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}