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6 results on '"Friederike Ewald"'

1. The Extremely Brilliant Source storage ring of the European Synchrotron Radiation Facility

Author

Pantaleo Raimondi, Chamseddine Benabderrahmane, Paul Berkvens, Jean Claude Biasci, Pawel Borowiec, Jean-Francois Bouteille, Thierry Brochard, Nicholas B. Brookes, Nicola Carmignani, Lee R. Carver, Jean-Michel Chaize, Joel Chavanne, Stefano Checchia, Yuriy Chushkin, Filippo Cianciosi, Marco Di Michiel, Rudolf Dimper, Alessandro D’Elia, Dieter Einfeld, Friederike Ewald, Laurent Farvacque, Loys Goirand, Laurent Hardy, Jorn Jacob, Laurent Jolly, Michael Krisch, Gael Le Bec, Isabelle Leconte, Simone M. Liuzzo, Cristian Maccarrone, Thierry Marchial, David Martin, Mohamed Mezouar, Christian Nevo, Thomas Perron, Eric Plouviez, Harald Reichert, Pascal Renaud, Jean-Luc Revol, Benoît Roche, Kees-Bertus Scheidt, Vincent Serriere, Francesco Sette, Jean Susini, Laura Torino, Reine Versteegen, Simon White, and Federico Zontone

Subjects
Astrophysics, QB460-466, Physics, QC1-999
Abstract

Abstract The Extremely Brilliant Source (EBS) is the experimental implementation of the novel Hybrid Multi Bend Achromat (HMBA) storage ring magnetic lattice concept, which has been realised at European Synchrotron Radiation Facility. We present its successful commissioning and first operation. We highlight the strengths of the HMBA design and compare them to the previous designs, on which most operational synchrotron X-ray sources are based. We report on the EBS storage ring’s significantly improved horizontal electron beam emittance and other key beam parameters. EBS extends the reach of synchrotron X-ray science confirming the HMBA concept for future facility upgrades and new constructions.

Published
2023
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3. Unique biofilm signature, drug susceptibility and decreased virulence in Drosophila through the Pseudomonas aeruginosa two-component system PprAB.

Author

Sophie de Bentzmann, Caroline Giraud, Christophe S Bernard, Virginie Calderon, Friederike Ewald, Patrick Plésiat, Cathy Nguyen, Didier Grunwald, Ina Attree, Katy Jeannot, Marie-Odile Fauvarque, and Christophe Bordi

Subjects
Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5
Abstract

Bacterial biofilm is considered as a particular lifestyle helping cells to survive hostile environments triggered by a variety of signals sensed and integrated through adequate regulatory pathways. Pseudomonas aeruginosa, a Gram-negative bacterium causing severe infections in humans, forms biofilms and is a fantastic example for fine-tuning of the transition between planktonic and community lifestyles through two-component systems (TCS). Here we decipher the regulon of the P. aeruginosa response regulator PprB of the TCS PprAB. We identified genes under the control of this TCS and once this pathway is activated, analyzed and dissected at the molecular level the PprB-dependent phenotypes in various models. The TCS PprAB triggers a hyper-biofilm phenotype with a unique adhesive signature made of BapA adhesin, a Type 1 secretion system (T1SS) substrate, CupE CU fimbriae, Flp Type IVb pili and eDNA without EPS involvement. This unique signature is associated with drug hyper-susceptibility, decreased virulence in acutely infected flies and cytotoxicity toward various cell types linked to decreased Type III secretion (T3SS). Moreover, once the PprB pathway is activated, decreased virulence in orally infected flies associated with enhanced biofilm formation and dissemination defect from the intestinal lumen toward the hemolymph compartment is reported. PprB may thus represent a key bacterial adaptation checkpoint of multicellular and aggregative behavior triggering the production of a unique matrix associated with peculiar antibiotic susceptibility and attenuated virulence, a particular interesting breach for therapeutic intervention to consider in view of possible eradication of P. aeruginosa biofilm-associated infections.

Published
2012
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4. Unique biofilm signature, drug susceptibility and decreased virulence in Drosophila through the Pseudomonas aeruginosa two-component system PprAB

Author

Friederike Ewald, Cathy Nguyen, Marie-Odile Fauvarque, Ina Attree, Virginie Calderon, Katy Jeannot, Sophie de Bentzmann, Christophe Bordi, Christophe S. Bernard, Didier Grunwald, Patrick Plésiat, Caroline Giraud, Laboratoire d'ingénierie des systèmes macromoléculaires (LISM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU), Laboratoire de microbiologie et génétique moléculaires (LMGM), Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de bactériologie, Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Technologies avancées pour le génôme et la clinique (TAGC), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), ANTE-INSERM U836, équipe 4, Muscles et pathologies, Biologie du Cancer et de l'Infection (BCI ), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), French cystic fibrosis foundation, French Ministry of Research and Technology, Region Rhône-Alpes, European Project, Roux-Buisson, Nathalie, ERA-NET ADHRES 27481, INCOMING, Laboratoire de microbiologie et génétique moléculaires - UMR5100 (LMGM), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Université Bourgogne Franche-Comté [COMUE] (UBFC), Theories and Approaches of Genomic Complexity (TAGC), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Pathogénie bactérienne et réponses cellulaires, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherches en Technologies et Sciences pour le Vivant (IRTSV), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
MESH: Adhesins, Bacterial, Fimbria, Pathogenesis, medicine.disease_cause, MESH: Animals, Biology (General), MESH: Bacterial Secretion Systems, Bacterial Secretion Systems, ComputingMilieux_MISCELLANEOUS, 0303 health sciences, Genomics, 3. Good health, Bacterial Pathogens, Host-Pathogen Interaction, Drosophila melanogaster, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Pseudomonas aeruginosa, MESH: Pseudomonas aeruginosa, Research Article, QH301-705.5, Immunology, Virulence, MESH: Biofilms, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Microbiology, Bacterial genetics, Cell Line, MESH: Drosophila melanogaster, MESH: Fimbriae, Bacterial, 03 medical and health sciences, Virology, medicine, Genetics, Animals, Secretion, Adhesins, Bacterial, Molecular Biology, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, [SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology, 030304 developmental biology, 030306 microbiology, fungi, Biofilm, Bacteriology, RC581-607, MESH: Cell Line, Bacterial adhesin, Regulon, Biofilms, Fimbriae, Bacterial, Parasitology, Immunologic diseases. Allergy
Abstract

Bacterial biofilm is considered as a particular lifestyle helping cells to survive hostile environments triggered by a variety of signals sensed and integrated through adequate regulatory pathways. Pseudomonas aeruginosa, a Gram-negative bacterium causing severe infections in humans, forms biofilms and is a fantastic example for fine-tuning of the transition between planktonic and community lifestyles through two-component systems (TCS). Here we decipher the regulon of the P. aeruginosa response regulator PprB of the TCS PprAB. We identified genes under the control of this TCS and once this pathway is activated, analyzed and dissected at the molecular level the PprB-dependent phenotypes in various models. The TCS PprAB triggers a hyper-biofilm phenotype with a unique adhesive signature made of BapA adhesin, a Type 1 secretion system (T1SS) substrate, CupE CU fimbriae, Flp Type IVb pili and eDNA without EPS involvement. This unique signature is associated with drug hyper-susceptibility, decreased virulence in acutely infected flies and cytotoxicity toward various cell types linked to decreased Type III secretion (T3SS). Moreover, once the PprB pathway is activated, decreased virulence in orally infected flies associated with enhanced biofilm formation and dissemination defect from the intestinal lumen toward the hemolymph compartment is reported. PprB may thus represent a key bacterial adaptation checkpoint of multicellular and aggregative behavior triggering the production of a unique matrix associated with peculiar antibiotic susceptibility and attenuated virulence, a particular interesting breach for therapeutic intervention to consider in view of possible eradication of P. aeruginosa biofilm-associated infections., Author Summary We unraveled that once the two-component system PprAB regulatory pathway is activated, Pseudomonas aeruginosa displays a unique hyper-biofilm phenotype due to a molecular signature combining a T1SS high molecular weight substrate, BapA, fimbriae of the chaperone-usher pathway, Type IVb pili and eDNA. Originally, this particular hyper-biofilm that is not strictly dependent on Psl or Pel exopolysaccharide (EPS) synthesis displays increased drug susceptibility, in contrary to previously reported biofilm lifestyle associated with increased resistance to antibiotics. PprB-dependent hyper-biofilm was also observed on intestinal mucosa of orally infected Drosophila flies in which it also displays a reduced capacity to cross the epithelial barrier from the intestinal lumen toward the hemolymph that consequently resulted in a reduced capacity to kill flies. Furthermore, constitutive activation of this PprB regulatory pathway triggers a reduced secretion of T3SS effectors which may account for the decreased virulence observed in epithelial and macrophage lineages and in acute Drosophila infections induced by septic injury. We appended in this study pieces of regulatory and molecular data that highlight the possibility to combat infections due to P. aeruginosa-biofilm with particular matrix.

Published
2012

5. Chopper system for time resolved experiments with synchrotron radiation

Author

Philip A. Anfinrud, Maciej Lorenc, Stephan Polachowski, Marco Cammarata, Friederike Ewald, Anton Plech, Bernd Lindenau, Michael Wulff, Jürgen Räbiger, Wolfgang Reichenbach, Qingyu Kong, Friedrich Schotte, Laurent Eybert, European Synchrotron Radiation Facility (ESRF), Laboratory of Chemical Physics [Bethesda] (LCP), National Institutes of Health, Institute for Synchrotron Radiation (ISS), Forschungszentrum Karlsruhe, Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Institut de Physique de Rennes (IPR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS), Central Technology Division (ZAT), Forschungszentrum Jülich GmbH | Centre de recherche de Juliers, Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association, and Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)

Subjects
030303 biophysics, Synchrotron radiation, 02 engineering and technology, 7. Clean energy, law.invention, Chopper, 03 medical and health sciences, Optics, law, Shutter, Instrumentation, Physics, 0303 health sciences, high-speed techniques, X-ray apparatus, business.industry, synchrotron radiation, 07.85.-m X- and γ-ray instruments, 82.53.Kp Coherent spectroscopy of atoms and molecules, 82.53.Hn Pump probe experiments with bound states, Lasers, X-Rays, 021001 nanoscience & nanotechnology, Laser, Synchrotron, Pulse (physics), Beamline, beam choppers, 0210 nano-technology, business, Ultrashort pulse, Synchrotrons
Abstract

10 pages; International audience; A chopper system for time resolved pump-probe experiments with x-ray beams from a synchrotron is described. The system has three parts: a water-cooled heatload chopper, a high-speed chopper, and a millisecond shutter. The chopper system, which is installed in beamline ID09B at the European Synchrotron Radiation Facility, provides short x-ray pulses for pump-probe experiments with ultrafast lasers. The chopper system can produce x-ray pulses as short as 200 ns in a continuous beam and repeat at frequencies from 0 to 3 kHz. For bunch filling patterns of the synchrotron with pulse separations greater than 100 ns, the high-speed chopper can isolate single 100 ps x-ray pulses that are used for the highest time resolution. A new rotor in the high-speed chopper is presented with a single pulse (100 ps) and long pulse (10 μs) option. In white beam experiments, the heatload of the (noncooled) high-speed chopper is lowered by a heatload chopper, which absorbs 95% of the incoming power without affecting the pulses selected by the high speed chopper.

Published
2009

6. Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

Author

Michael Wulff, Jungkweon Choi, Antonio Cupane, Friedrich Schotte, Hyotcherl Ihee, Friederike Ewald, Matteo Levantino, Philip A. Anfinrud, Marco Cammarata, CAMMARATA, M, LEVANTINO, M, SCHOTTE, F, ANFINRUD, PA, EWALD, F, CHOI, J, CUPANE, A, WULFF, M, and IHEE, H

Subjects
Materials science, Protein Conformation, Crystallography, X-Ray, Biochemistry, Sensitivity and Specificity, Article, chemistry.chemical_compound, Hemoglobins, Protein structure, Scattering, Radiation, Spectroscopy, Wide-angle X-ray scattering, Molecular Biology, protein dynamics, conformational changes, hemoglobin, myoglobin, cytochrome c, Scattering, Myoglobin, X-Rays, Resolution (electron density), Cytochromes c, Cell Biology, Nanosecond, chemistry, Chemical physics, Protein quaternary structure, sense organs, Biotechnology
Abstract

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Published
2008

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