Bouhedda F., Ryckelynck M.
Compartmentalization-based technologies for in vitro selection and evolution of ribozymes and light-up RNA aptamers Chapitre d'ouvrage
Dans: & B. Masquida S. Müller, W. Winkler (Ed.): Ribozymes, vol. 28, p. 721-738, John Wiley & Sons, Ltd, 2021.
Résumé | Liens | BibTeX | Étiquettes: catalytic RNAs, Droplet microfluidics, fluorescence, in vitro evolution, In vitro selection, light-up RNA aptamers, ribozymes, RYCKELYNCK, screening, Unité ARN
@inbook{nokey,
title = {Compartmentalization-based technologies for in vitro selection and evolution of ribozymes and light-up RNA aptamers},
author = {F. Bouhedda and M. Ryckelynck},
editor = {W. Winkler & B. Masquida S. Müller},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/9783527814527.ch28},
doi = {10.1002/9783527814527.ch28},
year = {2021},
date = {2021-01-01},
booktitle = {Ribozymes},
volume = {28},
pages = {721-738},
publisher = {John Wiley & Sons, Ltd},
abstract = {Summary Catalytic RNAs, also known as ribozymes, are naturally found in every living cell where they can occupy functions as important as peptide bond formation catalysis or intron splicing just as two examples. Besides, ribozymes are thought to be very ancient molecules that might have been the key actors of the so-called RNA world, but they also hold great promise for plenty of modern applications. These features have stimulated the development of in vitro evolution methodologies aiming at characterizing existing but also isolate new artificial ribozymes. Whereas bulk approaches in which all the RNA sequences of library are assayed in a single reaction mixture may be efficient to select fast, single-turn-over and/or self-modifying catalysts, this format is less adapted to the isolation of multiple turnover trans-acting molecules. Instead, a compartmentalization approach in which each variant is isolated and assayed into an individual compartment is better suited. In this chapter, we review the different strategies available to perform such compartmentalization and that range from hand-made water-in-oil emulsion to more advanced microfluidic-assisted ultrahigh-throughput screening. We finally extend the applications scope of these technologies to other RNAs (i.e., light-up RNA aptamers) for which a functional screening may also reveal more efficient than more conventional bulk in vitro selections.},
keywords = {catalytic RNAs, Droplet microfluidics, fluorescence, in vitro evolution, In vitro selection, light-up RNA aptamers, ribozymes, RYCKELYNCK, screening, Unité ARN},
pubstate = {published},
tppubtype = {inbook}
}
Schaeffer Evelyne, Dehuyser Laure, Sigwalt David, Flacher Vincent, Bernacchi Serena, Chaloin Olivier, Remy Jean-Serge, Mueller Christopher G, Baati Rachid, Wagner Alain
Dynamic micelles of mannoside glycolipids are more efficient than polymers for inhibiting HIV-1 trans-infection Article de journal
Dans: Bioconjugate Chemistry, vol. 24, no. 11, p. 1813–1823, 2013, ISSN: 1520-4812.
Résumé | Liens | BibTeX | Étiquettes: Anti-HIV Agents, Calcium, Cells, Chemistry, Cultured, Dendritic Cells, Dose-Response Relationship, Drug, Electron, fluorescence, Glycolipids, HIV, HIV Infections, HIV-1, Human, Humans, immunodeficiency, immunopathology, inhibition, LECTIN, Lectins, lipid, Mannosides, Micelles, Microbial Sensitivity Tests, Microscopy, Models, Molecular, Molecular Structure, Polymers, prophylaxis, Spectrometry, Structure-Activity Relationship, Surface Plasmon Resonance, target, Team-Mueller, Thermodynamics, Transmission, virus
@article{schaeffer_dynamic_2013,
title = {Dynamic micelles of mannoside glycolipids are more efficient than polymers for inhibiting HIV-1 trans-infection},
author = {Evelyne Schaeffer and Laure Dehuyser and David Sigwalt and Vincent Flacher and Serena Bernacchi and Olivier Chaloin and Jean-Serge Remy and Christopher G Mueller and Rachid Baati and Alain Wagner},
doi = {10.1021/bc4000806},
issn = {1520-4812},
year = {2013},
date = {2013-11-01},
journal = {Bioconjugate Chemistry},
volume = {24},
number = {11},
pages = {1813--1823},
abstract = {Mannoside glycolipid conjugates are able to inhibit human immunodeficiency virus type 1 (HIV-1) trans-infection mediated by human dendritic cells (DCs). The conjugates are formed by three building blocks: a linear or branched mannose head, a hydrophilic linker, and a 24-carbon lipid chain. We have shown that, even as single molecules, these compounds efficiently target mannose-binding lectins, such as DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN) important for HIV-1 transmission. With the goal to optimize their inhibitory activity by supramolecular structure formation, we have compared saturated and unsaturated conjugates, as single molecules, self-assemblies of dynamic micelles, and photopolymerized cross-linked polymers. Surface plasmon resonance showed that, unexpectedly, polymers of trivalent conjugates did not display a higher binding affinity for DC-SIGN than single molecules. Interactions on a chip or in solution were independent of calcium; however, binding to DCs was inhibited by a calcium chelator. Moreover, HIV-1 trans-infection was mostly inhibited by dynamic micelles and not by rigid polymers. The inhibition data revealed a clear correlation between the structure and molecular assembly of a conjugate and its biological antiviral activity. We present an interaction model between DC-SIGN and conjugates-either single molecules, micelles, or polymers-that highlights that the most effective interactions by dynamic micelles involve both mannose heads and lipid chains. Our data reveal that trivalent glycolipid conjugates display the highest microbicide potential for HIV prophylaxis, as dynamic micelles conjugates and not as rigid polymers.},
keywords = {Anti-HIV Agents, Calcium, Cells, Chemistry, Cultured, Dendritic Cells, Dose-Response Relationship, Drug, Electron, fluorescence, Glycolipids, HIV, HIV Infections, HIV-1, Human, Humans, immunodeficiency, immunopathology, inhibition, LECTIN, Lectins, lipid, Mannosides, Micelles, Microbial Sensitivity Tests, Microscopy, Models, Molecular, Molecular Structure, Polymers, prophylaxis, Spectrometry, Structure-Activity Relationship, Surface Plasmon Resonance, target, Team-Mueller, Thermodynamics, Transmission, virus},
pubstate = {published},
tppubtype = {article}
}
Nehme Nadine T, Liégeois Samuel, Kele Beatrix, Giammarinaro Philippe, Pradel Elizabeth, Hoffmann Jules A, Ewbank Jonathan J, Ferrandon Dominique
A model of bacterial intestinal infections in Drosophila melanogaster Article de journal
Dans: PLoS Pathog., vol. 3, no. 11, p. e173, 2007, ISSN: 1553-7374.
Résumé | Liens | BibTeX | Étiquettes: Animal, Animals, Disease Models, Electron, ferrandon, fluorescence, Hemolymph, hoffmann, Host-Pathogen Interactions, Immunohistochemistry, Intestines, M3i, Microscopy, Reverse Transcriptase Polymerase Chain Reaction, Serratia Infections, Serratia marcescens, Transmission
@article{nehme_model_2007b,
title = {A model of bacterial intestinal infections in Drosophila melanogaster},
author = {Nadine T Nehme and Samuel Liégeois and Beatrix Kele and Philippe Giammarinaro and Elizabeth Pradel and Jules A Hoffmann and Jonathan J Ewbank and Dominique Ferrandon},
doi = {10.1371/journal.ppat.0030173},
issn = {1553-7374},
year = {2007},
date = {2007-01-01},
journal = {PLoS Pathog.},
volume = {3},
number = {11},
pages = {e173},
abstract = {Serratia marcescens is an entomopathogenic bacterium that opportunistically infects a wide range of hosts, including humans. In a model of septic injury, if directly introduced into the body cavity of Drosophila, this pathogen is insensitive to the host's systemic immune response and kills flies in a day. We find that S. marcescens resistance to the Drosophila immune deficiency (imd)-mediated humoral response requires the bacterial lipopolysaccharide O-antigen. If ingested by Drosophila, bacteria cross the gut and penetrate the body cavity. During this passage, the bacteria can be observed within the cells of the intestinal epithelium. In such an oral infection model, the flies succumb to infection only after 6 days. We demonstrate that two complementary host defense mechanisms act together against such food-borne infection: an antimicrobial response in the intestine that is regulated by the imd pathway and phagocytosis by hemocytes of bacteria that have escaped into the hemolymph. Interestingly, bacteria present in the hemolymph elicit a systemic immune response only when phagocytosis is blocked. Our observations support a model wherein peptidoglycan fragments released during bacterial growth activate the imd pathway and do not back a proposed role for phagocytosis in the immune activation of the fat body. Thanks to the genetic tools available in both host and pathogen, the molecular dissection of the interactions between S. marcescens and Drosophila will provide a useful paradigm for deciphering intestinal pathogenesis.},
keywords = {Animal, Animals, Disease Models, Electron, ferrandon, fluorescence, Hemolymph, hoffmann, Host-Pathogen Interactions, Immunohistochemistry, Intestines, M3i, Microscopy, Reverse Transcriptase Polymerase Chain Reaction, Serratia Infections, Serratia marcescens, Transmission},
pubstate = {published},
tppubtype = {article}
}
Lacerda L, Pastorin G, Gathercole D, Buddle J, Prato M, Bianco A, Kostarelos K
Intracellular Trafficking of Carbon Nanotubes by Confocal Laser Scanning Microscopy Article de journal
Dans: Advanced Materials, vol. 19, no. 14, p. 1789–1789, 2007, ISSN: 1521-4095.
Liens | BibTeX | Étiquettes: Biomedical materials, Cells, Drug delivery, fluorescence, I2CT, Nanotubes, single-walled, Team-Bianco
@article{lacerda_intracellular_2007,
title = {Intracellular Trafficking of Carbon Nanotubes by Confocal Laser Scanning Microscopy},
author = {L Lacerda and G Pastorin and D Gathercole and J Buddle and M Prato and A Bianco and K Kostarelos},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/adma.200790051},
doi = {10.1002/adma.200790051},
issn = {1521-4095},
year = {2007},
date = {2007-01-01},
urldate = {2020-03-31},
journal = {Advanced Materials},
volume = {19},
number = {14},
pages = {1789--1789},
keywords = {Biomedical materials, Cells, Drug delivery, fluorescence, I2CT, Nanotubes, single-walled, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Briand Jean-Paul, Prato Maurizio, Bianco Alberto
Translocation of bioactive peptides across cell membranes by carbon nanotubes Article de journal
Dans: Chemical Communications (Cambridge, England), no. 1, p. 16–17, 2004, ISSN: 1359-7345.
Résumé | Liens | BibTeX | Étiquettes: 3T3 Cells, Animals, carbon, Cell Membrane, Confocal, Flow Cytometry, fluorescence, I2CT, Mice, Microscopy, Nanotubes, Particle Size, Peptides, Protein Transport, Team-Bianco
@article{pantarotto_translocation_2004,
title = {Translocation of bioactive peptides across cell membranes by carbon nanotubes},
author = {Davide Pantarotto and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1039/b311254c},
issn = {1359-7345},
year = {2004},
date = {2004-01-01},
journal = {Chemical Communications (Cambridge, England)},
number = {1},
pages = {16--17},
abstract = {Functionalised carbon nanotubes are able to cross the cell membrane and to accumulate in the cytoplasm or reach the nucleus without being toxic for the cell up to 10 [micro sign]M.},
keywords = {3T3 Cells, Animals, carbon, Cell Membrane, Confocal, Flow Cytometry, fluorescence, I2CT, Mice, Microscopy, Nanotubes, Particle Size, Peptides, Protein Transport, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Rosenthal G A, Reichhart Jean-Marc, Hoffmann Jules A
L-canavanine incorporation into vitellogenin and macromolecular conformation Article de journal
Dans: J. Biol. Chem., vol. 264, no. 23, p. 13693–13696, 1989, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Antibodies, Canavanine, fluorescence, Grasshoppers, hoffmann, M3i, Monoclonal, Protein Conformation, reichhart, Spectrometry, Vitellogenins
@article{rosenthal_l-canavanine_1989,
title = {L-canavanine incorporation into vitellogenin and macromolecular conformation},
author = {G A Rosenthal and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {0021-9258},
year = {1989},
date = {1989-01-01},
journal = {J. Biol. Chem.},
volume = {264},
number = {23},
pages = {13693--13696},
abstract = {L-Canavanine is a potentially deleterious arginine antimetabolite whose toxicity is expressed in canavanine-sensitive organisms ranging from viruses to humans. Canavanine, a substrate for arginyl-tRNA synthetase, is incorporated into nascent polypeptide chains in place of arginine. This substitution results in the production of structurally aberrant, canavanyl proteins. Chemical, physical, and immunological studies of native and canavanine-containing vitellogenin obtained from female migratory locusts (Locusta migratoria migratorioides (Orthoptera] provide the first experimental evidence that canavanine can disrupt the tertiary and/or quaternary structure that yields the three-dimensional conformation unique to the protein. These findings enhance our understanding of the biochemical basis for canavanine's antimetabolic and potent insecticidal properties.},
keywords = {Animals, Antibodies, Canavanine, fluorescence, Grasshoppers, hoffmann, M3i, Monoclonal, Protein Conformation, reichhart, Spectrometry, Vitellogenins},
pubstate = {published},
tppubtype = {article}
}