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1. Ferromagnetic resonance in the complex permeability of an Fe$_3$O$_4$ nanosuspension at radio and microwave frequencies

Author

Dubreuil, J. and Bobowski, J. S.

Subjects
Condensed Matter - Mesoscale and Nanoscale Physics, Physics - Applied Physics
Abstract

The complex permeability of an iron-oxide nanosuspension has been measured as a function of magnetic field strength at RF and microwave frequencies using a loop-gap resonator. The particles were suspended in water and had an 8-nm diameter Fe$_3$O$_4$ core that was coated by Dextran. The real part of the permeability increased sharply beyond a frequency-dependent threshold value of the static magnetic field before saturating. Just beyond this threshold field, there was a peak in the imaginary part of the permeability. The permeability measurements, which exhibited features associated with ferromagnetic resonance, were used to determine the dependence of the microwave absorption on static magnetic field strength. Using the absorption data, the $g$-factor of the nanosuspension was found to be $1.86\pm 0.07$., Comment: 7 pages, 6 figures

Published
2018
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22. List of Contributors

Author

Aktories, Klaus, primary, Alape-Girón, Alberto, additional, Barbier, Julien, additional, Barbieri, Joseph T., additional, Barth, Holger, additional, Basak, Ajit K., additional, Benz, Roland, additional, Bercsenyi, Kinga, additional, Bergan, Jonas, additional, Bergmann, Stefan, additional, Bezrukov, Sergey M., additional, Bjørnestad, Victoria A., additional, Boquet, Patrice, additional, Boyer, Laurent, additional, Bravo, Alejandra, additional, Bryant, Amy E., additional, Bumba, Ladislav, additional, Cantón, Pablo Emiliano, additional, Chenal, Alexandre, additional, Dal Peraro, Matteo, additional, de Souza Santos, Marcela, additional, Dobrindt, Ulrich, additional, Dolly, J. Oliver, additional, Dubreuil, J. Daniel, additional, Filloux, Alain, additional, Frank, Dara W., additional, Flores-Díaz, Marietta, additional, Fraser, John D., additional, Frisan, Teresa, additional, Galan, Jorge E., additional, García-Gómez, Blanca I., additional, Genth, Harald, additional, Gillet, Daniel, additional, Gómez, Isabel, additional, Granum, Per Einar, additional, Hacker, Jörg, additional, Harper, Callista B., additional, Heggelund, Julie E., additional, Ho, Mengfei, additional, Hotze, Eileen M., additional, Huyet, Jessica, additional, Iacovache, Ioan, additional, Jank, Thomas, additional, Jover, Emmanuel, additional, Just, Ingo, additional, Krachler, Anne-Marie, additional, Krengel, Ute, additional, Ladant, Daniel, additional, Langley, Ries J., additional, Lemichez, Emmanuel, additional, Leppla, Stephen H., additional, Li, Peng, additional, Lindbäck, Toril, additional, Lingelem, Anne Berit Dyve, additional, Liu, Shihui, additional, Locht, Camille, additional, de Castro, Diana L. Martínez, additional, Masin, Jiri, additional, McClane, Bruce A., additional, McCluskey, Adam, additional, Mendoza, Gretel, additional, Meunier, Frederic A., additional, Moayeri, Mahtab, additional, Molgó, Jordi, additional, Monturiol-Gross, Laura, additional, Munro, Patrick, additional, Naylor, Claire E., additional, Nestorovich, Ekaterina M., additional, Ocelotl, Josue, additional, Onofre, Janette, additional, Orth, Joachim H.C., additional, Orth, Kim, additional, Osicka, Radim, additional, Pacheco, Sabino, additional, Pomerantsev, Andrei P., additional, Popoff, Michel R., additional, Poulain, Bernard, additional, Prévost, Gilles, additional, Proft, Thomas, additional, Ricci, Vittorio, additional, Robinson, Phillip J., additional, Rolsma, Stephanie, additional, Roxas-Duncan, Virginia I., additional, Sagfors, Agnes, additional, Salomon, Dor, additional, Sánchez, Jorge, additional, Sandvig, Kirsten, additional, Savva, Christos, additional, Schiavo, Giampietro, additional, Schmidt, Gudula, additional, Schmieg, Nathalie, additional, Sebo, Peter, additional, Shah, Sadrick, additional, Shrestha, Archana, additional, Skotland, Tore, additional, Smith, Leonard A., additional, Soberón, Mario, additional, Sommi, Patrizia, additional, Sotomayor-Perez, A.C., additional, Stevens, Dennis L., additional, Stiles, Bradley G., additional, Tawk, Mira Y., additional, Titball, Richard, additional, Tjaden, Sarah, additional, Tweten, Rodney K., additional, van der Goot, Françoise Gisou, additional, Wade, Kristin R., additional, Wang, Jiafu, additional, Wilson, Brenda A., additional, and Zimmermann-Meisse, Gaëlle, additional

Published
2015
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25. Isolation and characterization of [alpha]-enolase, a novel fibronectin-binding protein from Streptococcus suis

Author

Esgleas, Miriam, Li, Yuanyi, Hancock, Mark A., Harel, Josee, Dubreuil, J. Daniel, and Gottschalk, Marcelo

Subjects
Enolase -- Physiological aspects, Enolase -- Properties, Enolase -- Identification and classification, Fibronectins -- Physiological aspects, Streptococcus -- Physiological aspects, Streptococcus -- Research, Biological sciences
Abstract

Streptococcus suis is an important swine pathogen that causes meningitis, endocarditis, arthritis and septicaemia. As a zoonotic agent, S. suis also causes similar diseases in humans. Binding of pathogenic bacteria to extracellular matrix components enhances their adhesion to and invasion of host cells. In the present study we isolated and identified a novel fibronectin-binding protein from S. suis. The native protein (designated SsEno) possessed not only high homology with other bacterial enolases but also enolase activity. We cloned, expressed and purified SsEno and showed that it is ubiquitously expressed by all S. suis serotypes and we identified its surface localization using immunoelectron microscopy. ELISA demonstrated that SsEno binds specifically to fibronectin and plasminogen in a lysine-dependent manner. Additional surface plasmon resonance assays demonstrated that SsEno binds to fibronectin or plasminogen with low nanomolar affinity. Inhibition experiments with anti-SsEno antibodies also showed that bacterial SsEno is important for the adhesion to and invasion of brain microvascular endothelial cells by S. suis. Overall, the present work is the first study, to our knowledge, to demonstrate a fibronectin-binding activity of a bacterial enolase, and shows that, similar to other bacterial fibronectin-binding proteins, SsEno may contribute to the virulence of S. suis.

Published
2008

26. Modulation of hexa-acyl pyrophosphate lipid A population under Escherichia coli phosphate (Pho) regulon activation

Author

Lamarche, Martin G., Kim, Sang-Hyun, Crepin, Sebastien, Mourez, Michael, Bertrand, Nicolas, Bishop, Russell E., Dubreuil, J. Daniel, and Harel, Josee

Subjects
Escherichia coli -- Physiological aspects, Pyrophosphates -- Genetic aspects, Pyrophosphates -- Physiological aspects, Genetic regulation -- Physiological aspects, Biological sciences
Abstract

Environmental phosphate is an important signal for microorganism gene regulation, and it has recently been shown to trigger some key bacterial virulence mechanisms. In many bacteria, the Pho regulon is the major circuit involved in adaptation to phosphate limitation. The Pho regulon is controlled jointly by the two-component regulatory system PhoR/PhoB and by the phosphate-specific transport (Pst) system, which both belong to the Pho regulon. We showed that a pst mutation results in virulence attenuation in extraintestinal pathogenic Escherichia coli (ExPEC) strains. Our results indicate that the bacterial cell surface of the pst mutants is altered. In this study, we show that pst mutants of ExPEC strains display an increased sensitivity to different cationic antimicrobial peptides and vancomycin. Remarkably, the hexa-acylated 1-pyrophosphate form of lipid A is significantly less abundant in pst mutants. Among differentially expressed genes in the pst mutant, 1pxT coding for an enzyme that transfers a phosphoryl group to lipid A, forming the 1-diphosphate species, was found to be downregulated. Our results strongly suggest that the Pho regulon is involved in lipid A modifications, which could contribute to bacterial surface perturbations. Since the Pho regulon and the Pst system are conserved in many bacteria, such a lipid A modification mechanism could be widely distributed among gram-negative bacterial species.

Published
2008

29. Binding to sulfatide and enterotoxicity of various Escherichia coli STb mutants

Author

Labrie, Vincent, Beausoleil, Hans-Erick, Harel, Josee, and Dubreuil, J. Daniel

Subjects
Microbiological research -- Analysis, Escherichia coli -- Genetic aspects, Gene mutations -- Physiological aspects, Enterotoxins -- Physiological aspects, Polypeptides -- Physiological aspects, Amino acids -- Physiological aspects, Biological sciences
Abstract

Research has been conducted on the amino acid polypeptide of the heat-stable Escherichia coli enterotoxin b. The role of the selected amino acids in the enterotoxicity and the involvement of these amino acids in the interactions of enterotoxin b with the functional receptor sulfatide have been investigated.

Published
2001

34. Escherichia coli STB enterotoxin

Author

Dubreuil, J. Daniels

Subjects
Escherichia coli -- Research, Enterotoxins -- Research, Bacteria, Pathogenic -- Research, Biological sciences
Abstract

Escherichia coli STb enterotoxin has been linked to diarrhoea illnesses of porcine origin. However, STb gene was alo found to be present in bovine, chicken and even human enterotoxigenic E. coli (ETEC) strains. STb has been documented as having effects on intestinal tissue through two possible mechanisms. It mediates the level of prostaglandin E2 which regulates water and electrolyte in diarhoea. The second mechanism involves the receptor-operative calcium channel in the plasma membrane.

Published
1997

36. Characterization of Streptococcus suis capsular type 2 haemolysin

Author

Gottschalk, Marcelo G., Lacouture, Sonia, and Dubreuil, J. Daniel

Subjects
Streptococcus -- Research, Bacterial toxins -- Research, Biological sciences
Abstract

Affinity chromatography of the haemolysin toxin from Streptococcus suis type 2 using a thiopropyl Sepharose 6B column reveals that the extracellular protein has a molecular mass of 65 kDa. The haemolysin's response to oxygen and oxidizing agents, suppression by low levels of cholesterol, stimulation by reducing agents and transmembrane pore formation enable its classification into a family of antigenically related cholesterol-binding cytolytic toxins. S. suis haemolysin haemolytic activity is prevented by anti-streptolysin antibodies.

Published
1995

37. Fusion of the genes encoding Escherichia coli heat-stable enterotoxin b (STb) and the maltose-binding protein to obtain mature STb enterotoxin

Author

Bosse, Marc, Handl, Carina E., Lortie, Louis-Andre, Harel, Josee, and Dubreuil, J. Daniel

Subjects
Escherichia coli -- Genetic aspects, Enterotoxins -- Genetic aspects, Recombinant proteins -- Research, Biological sciences
Abstract

The enterotoxigenic Escherichia coli estB gene codes for the heat-stable entrotoxin b (STb) associated with swine diarrhea. To overexpress STb, the estB gene was fused to the malB gene coding for a maltose-binding protein and the construct was placed under the control of a strong promoter. Expression of the hybrid plasmid resulted in the synthesis of the fusion protein in the periplasm of E. coli. The STb portion of the fusion protein could be recovered by cleavage with Xa protease.

Published
1993

42. Cytoreductive surgery and hyperthermic intraperitoneal chemotherapy for pseudomyxoma peritonei of appendicular and extra-appendicular origin

Author

Delhorme, J-B, primary, Severac, F, additional, Averous, G, additional, Glehen, O, additional, Passot, G, additional, Bakrin, N, additional, Marchal, F, additional, Pocard, M, additional, Lo Dico, R, additional, Eveno, C, additional, Carrere, S, additional, Sgarbura, O, additional, Quenet, F, additional, Ferron, G, additional, Goéré, D, additional, Brigand, C, additional, Abba, J, additional, Abboud, K, additional, Alyami, M, additional, Arvieux, C, additional, Balagué, G, additional, Barrau, V, additional, Ben Rejeb, H, additional, Bereder, J-M, additional, Berton-Rigaud, I, additional, Bibeau, F, additional, Bonnefoy, I, additional, Bouzard, D, additional, Bricault, I, additional, Carrère, S, additional, de Chaisemartin, C, additional, Chassang, M, additional, Chevallier, A, additional, Courvoisier, T, additional, Dartigues, P, additional, Dohan, A, additional, Dubreuil, J, additional, Dumont, F, additional, Faruch-Bilfeld, M, additional, Fontaine, J, additional, Fournier, L, additional, Gagniere, J, additional, Geffroy, D, additional, Ghouti, L, additional, Gilly, F-N, additional, Gladieff, L, additional, Guibal, A, additional, Guilloit, J-M, additional, Guyon, F, additional, Heyd, B, additional, Hoeffel, C, additional, Hordonneau, C, additional, Isaac, S, additional, Jourdan-Enfer, P, additional, Kaci, R, additional, Kianmanesh, R, additional, Labbé-Devilliers, C, additional, Lacroix, J, additional, Lelong, B, additional, Leroux-Broussier, A, additional, Lherm, Y, additional, Lorimier, G, additional, Malhaire, C, additional, Mariani, P, additional, Mathiotte, E, additional, Meeus, P, additional, Mery, E, additional, Msika, S, additional, Nadeau, C, additional, Ortega-Deballon, P, additional, Pellet, O, additional, Peyrat, P, additional, Pezet, D, additional, Pirro, N, additional, Poizat, F, additional, Porcheron, J, additional, Poulet, A, additional, Rat, P, additional, Rousselot, P, additional, Rousset, P, additional, Senellart, H, additional, Serrano, M, additional, Servois, V, additional, Sgabura, O, additional, Skanjeti, A, additional, Svrcek, M, additional, Tetreau, R, additional, Thibaudeau, E, additional, Touchefeu, Y, additional, Tuech, J-J, additional, Valmary-Degano, S, additional, Vaudoyer, D, additional, Velasco, S, additional, Verriele-Beurrier, V, additional, Villeneuve, L, additional, Wernert, R, additional, and Zinzindohoue, F, additional

Published
2018
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44. Immunohistochemical evaluation of two antibodies against PD-L1 and prognostic significance of PD-L1 expression in epithelioid peritoneal malignant mesothelioma: A RENAPE study

Author

Valmary-Degano, S., primary, Colpart, P., additional, Villeneuve, L., additional, Monnien, F., additional, M'Hamdi, L., additional, Lang Averous, G., additional, Capovilla, M., additional, Bibeau, F., additional, Laverriere, M.-H., additional, Verriele-Beurrier, V., additional, Ben Rejeb, H., additional, Dartigues, P., additional, Hommell-Fontaine, J., additional, Gilly, F.-N., additional, Isaac, S., additional, Mery, E., additional, Abba, J., additional, Abboud, K., additional, Alyami, M., additional, Arvieux, C., additional, Bakrin, N., additional, Balagué, G., additional, Barrau, V., additional, Bereder, J.-M., additional, Berton-Rigaud, I., additional, Bonnefoy, I., additional, Bouzard, D., additional, Bricault, I., additional, Brigand, C., additional, Carrère, S., additional, de Chaisemartin, C., additional, Chassang, M., additional, Chevallier, A., additional, Courvoisier, T., additional, Dohan, A., additional, Dromain, C., additional, Dubreuil, J., additional, Dumont, F., additional, Eveno, C., additional, Faruch-Bilfeld, M., additional, Ferron, G., additional, Fournier, L., additional, Gagniere, J., additional, Geffroy, D., additional, Ghouti, L., additional, Gladieff, L., additional, Glehen, O., additional, Goéré, D., additional, Guibal, A., additional, Guilloit, J.-M., additional, Guyon, F., additional, Heyd, B., additional, Hoeffel, C., additional, Hordonneau, C., additional, Jourdan-Enfer, P., additional, Kaci, R., additional, Kianmanesh, R., additional, Labbé-Devilliers, C., additional, Lacroix, J., additional, Lelong, B., additional, Leroux-Broussier, A., additional, Lherm, Y., additional, Lo Dico, R., additional, Lorimier, G., additional, Malhaire, C., additional, Marchal, F., additional, Mariani, P., additional, Mathiotte, E., additional, Meeus, P., additional, Msika, S., additional, Nadeau, C., additional, Ortega-Deballon, P., additional, Passot, G., additional, Pellet, O., additional, Peyrat, P., additional, Pezet, D., additional, Pirro, N., additional, Pocard, M., additional, Poizat, F., additional, Porcheron, J., additional, Poulet, A., additional, Quenet, F., additional, Rat, P., additional, Rousselot, P., additional, Senellart, H., additional, Serrano, M., additional, Servois, V., additional, Sgabura, O., additional, Skanjeti, A., additional, Svrcek, M., additional, Tetreau, R., additional, Thibaudeau, E., additional, Touchefeu, Y., additional, Tuech, J.-J., additional, Vaudoyer, D., additional, Velasco, S., additional, Wernert, R., additional, and Zinzindohoue, F., additional

Published
2017
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45. PROGNOSTIC MODEL FOR HIGH TUMOR BURDEN FOLLICULAR LYMPHOMA INCLUDING BASELINE TOTAL METABOLIC TUMOR VOLUME AND END INDUCTION PET: a POOLED ANALYSIS FROM LYSA AND FIL TRIALS

Author

Cottereau, A., primary, Versari, A., additional, Dupuis, J., additional, Chartier, L., additional, Menga, M., additional, Casasnovas, R., additional, Haioun, C., additional, Tilly, H., additional, Tarantino, V., additional, Dubreuil, J., additional, Federico, M., additional, Salles, G., additional, Luminari, S., additional, Trotman, J., additional, and Meignan, M., additional

Published
2017
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47. Helicobacter pylori interactions with host serum and extracellular matrix proteins: potential role in the infectious process

Author

Dubreuil, J. Daniel, Del Giudice, Giuseppe, and Rappuoli, Rino

Subjects
Microbiology -- Research, Molecular biology -- Research, Helicobacter pylori -- Genetic aspects, Helicobacter pylori -- Physiological aspects, Serum -- Physiological aspects, Bacterial proteins -- Genetic aspects, Bacterial proteins -- Physiological aspects, Virulence (Microbiology) -- Analysis, Biological sciences
Abstract

Thenauthors review the publications on Helicobacter pylori. The topics of interest include the interactions with host serum and interplay of H. pylori virulence factors resulting in cell damage.

Published
2002

48. Study of the Reinforced Concrete Structures Containment

Author

Nahas, G., Cirée, B., Quesada, M., Gelain, T., Loukili, A., Medgigbodo, G., Khelidj, A., Choinska, M., Regoin, J.P., Benboudjema, F., Darquennes, A., Hilaire, A., Bennacer, R., Rastiello, R., La Borderie, Christian, Lawrence, Claire, Dubreuil, J., Barbaroux, M.C., Gilliot, C., Institut de Radioprotection et de Sûreté Nucléaire (IRSN), Institut de Recherche en Génie Civil et Mécanique (GeM), Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-École Centrale de Nantes (ECN)-Centre National de la Recherche Scientifique (CNRS), Interactions Eau-Geomatériaux (IEG), Université de Nantes (UN)-Université de Nantes (UN)-École Centrale de Nantes (ECN)-Centre National de la Recherche Scientifique (CNRS)-Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-École Centrale de Nantes (ECN)-Centre National de la Recherche Scientifique (CNRS)-Institut Universitaire de Technologie Saint-Nazaire (IUT Saint-Nazaire), Université de Nantes (UN)-Université de Nantes (UN), Laboratoire de Mécanique et Technologie (LMT), École normale supérieure - Cachan (ENS Cachan)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Sciences de l'Ingénieur Appliquées à la Mécanique et au génie Electrique (SIAME), and Université de Pau et des Pays de l'Adour (UPPA)

Subjects
[PHYS]Physics [physics], ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2014

50. The Whole Shebang: The Gastrointestinal Tract, Escherichia coli Enterotoxins and Secretion

Author

Dubreuil, J. Daniel

Subjects
enterotoxigenic Escherichia coli, diarrhea, toxins, E. coli, gastrointestinal tract
Abstract

This review focuses on diarrhea caused by toxins released by enterotoxigenic Escherichia coli. These bacteria are known to produce toxins that have adverse effects on the intestinal tissue in Man and animals. E. coli is contracted through the ingestion of water or food contaminated by this bacterium. Generally, E. coli colonizes the intestinal mucosa where it multiplies and causes damage to the target cells or interferes with the homeostasis that prevails in the gastrointestinal tract. Enteropathogens such as E. coli are only able to exhibit their effects after colonization of the intestinal mucosa from where they release their toxins. These bacteria mainly affect chloride ions secretion through second messenger pathways resulting in secretory diarrhea. In this review, the association of bacteria with the gastrointestinal tract as pathogens and the resulting effects on the various systems of the intestine, including the nervous system and mediators leading to secretion and diarrhea are examined.

Published
2012
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