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26 results on '"MESH: Copper"'

1. Secreted pectin monooxygenases drive plant infection by pathogenic oomycetes

Author

Michael Csukai, Paul H. Walton, Lydia Welsh, Anna O. Avrova, Peter J. Lindley, Neil C. Bruce, Bernard Henrissat, Julie Squires, Gideon J. Davies, Stephen C. Whisson, Simon J. McQueen-Mason, Federico Sabbadin, Saioa Urresti, Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), University of York [York, UK], Instituto Biofisika, and Universidad del Pais Vasco / Euskal Herriko Unibertsitatea [Espagne] (UPV/EHU)-Consejo Superior de Investigaciones Científicas [Madrid] (CSIC)

Subjects
Models, Molecular, MESH: Oxidation-Reduction, 0106 biological sciences, Protein Conformation, [SDV]Life Sciences [q-bio], 01 natural sciences, Mixed Function Oxygenases, MESH: Protein Conformation, MESH: Plant Diseases, Solanum lycopersicum, MESH: Lycopersicon esculentum, Pathogen, 2. Zero hunger, Oomycete, 0303 health sciences, Multidisciplinary, biology, food and beverages, MESH: Mixed Function Oxygenases, MESH: Copper, MESH: Plant Leaves, Lytic cycle, Phytophthora infestans, Pectins, MESH: Protein Domains, Oxidation-Reduction, MESH: Models, Molecular, Virulence Factors, Virulence, MESH: Solanum tuberosum, Microbiology, Cell wall, 03 medical and health sciences, Protein Domains, Polysaccharides, Gene, Plant Diseases, Solanum tuberosum, MESH: Virulence Factors, 030304 developmental biology, Host (biology), fungi, biology.organism_classification, Plant Leaves, MESH: Polysaccharides, MESH: Phytophthora infestans, Copper, MESH: Pectins, 010606 plant biology & botany
Abstract

Potato pectin falls to Phytophthora Phytophthora infestans is a plant oomycete pathogen that drove the potato famines of the 1800s and continues to afflict potato fields today. The polysaccharide pectin makes up about a third of the cell wall in potatoes. Sabbadin et al . identified a family of lytic polysaccharide monooxygenases (LMPOs) that cleave pectin and are upregulated in P. infestans during infection. Silencing the relevant LMPO gene successfully inhibited P. infestans infections. These findings open doors for disease intervention targets and for biotech applications. —PJH

Published
2021

2. Leaching foams for copper and silver dissolution : a proof of concept of a more environmentally-friendly process for the recovery of critical metals

Author

Mengxue Zhang, Grégory Lefèvre, Alesya Mikhailovskaya, Pierre Trinh, Cécile Monteux, Nadège Pantoustier, Patrick Perrin, Sciences et Ingénierie de la Matière Molle (UMR 7615) (SIMM), Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche de Chimie Paris (IRCP), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Ministère de la Culture (MC), Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL), and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Ministère de la Culture (MC)

Subjects
MESH: Foams, Materials science, hydrometallurgy, General Chemical Engineering, 0211 other engineering and technologies, chemistry.chemical_element, MESH: Surfactants, metals, 02 engineering and technology, 010501 environmental sciences, recycling, 01 natural sciences, 7. Clean energy, 12. Responsible consumption, hydrometallurgy 2, Environmental Chemistry, [CHIM]Chemical Sciences, Dissolution, 021102 mining & metallurgy, 0105 earth and related environmental sciences, MESH: Metals, Renewable Energy, Sustainability and the Environment, Metallurgy, Foams, General Chemistry, Environmentally friendly, Copper, MESH: Copper, leaching, chemistry, 13. Climate action, Proof of concept, Scientific method, MESH: Bubbles, Leaching (metallurgy)
Abstract

International audience; The recovery of metals from WEEE, Waste from Electrical and Electronic Equipment, is a major challenge to preserve natural resources. Hydrometallurgy, which consists in leaching metals is a promising method but generates large amounts of polluting effluents. In this study we design aqueous leaching foams, composed of 90% v/v of gas and 10% v/v of HCl solution to oxidize and dissolve copper. We take advantage of the oxidizing power of the dioxygen (O2) present in the air bubbles whose fast transfer through the foams enables an efficient oxidation of copper. We then extend the concept of leaching foams to another gas, ozone, to oxidize silver (Ag). We finally show that using an anionic surfactant to complex cupric ions helps improving the dissolution of the metal. These promising results open new recycling routes for metals contained in WEEE, with a lower environmental footprint.

Published
2021

3. Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates

Author

Simmons, T. J., Frandsen, K. E. H., Ciano, L., Tryfona, T., Lenfant, N., Poulsen, J. C., Wilson, L. F. L., Tandrup, T., Tovborg, M., Schnorr, K., Johansen, K. S., Henrissat, B., Walton, P. H., Lo Leggio, L, Dupree, P., Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), UK Biotechnology and Biological Sciences Research Council BB/L000423/1 BB/L021633/1, Danish Council for Strategic Research 12-134923 12-134922, and European Project: 283570,EC:FP7:INFRA,FP7-INFRASTRUCTURES-2011-1,BIOSTRUCT-X(2011)

Subjects
Models, Molecular, MESH: Sordariales, Polysaccharides/chemistry, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Sordariales, MESH: Catalytic Domain, Mixed Function Oxygenases/chemistry, [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity, Mixed Function Oxygenases, Substrate Specificity, Polyporaceae, enzyme lytique, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Catalytic Domain, lcsh:Science, [SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases, Vegetal Biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Polyporaceae/enzymology, monooxygénase, MESH: Mixed Function Oxygenases, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], MESH: Copper, glucomannane, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], xyloglucane, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Copper/chemistry, MESH: Fungal Proteins, MESH: Models, Molecular, Fungal Proteins/chemistry, Science, Article, Fungal Proteins, MESH: Polyporaceae, Polysaccharides, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Electron Spin Resonance Spectroscopy, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Sordariales/enzymology, carbohydrates (lipids), MESH: Polysaccharides, polysaccharide, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, MESH: Electron Spin Resonance Spectroscopy, lcsh:Q, MESH: Substrate Specificity, Biologie végétale, Copper
Abstract

Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a functional and structural characterization of two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) and Collariella virescens (CvAA9A). LsAA9A and CvAA9A cleave a range of polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan and glucomannan. LsAA9A additionally cleaves isolated xylan substrates. The structures of CvAA9A and of LsAA9A bound to cellulosic and non-cellulosic oligosaccharides provide insight into the molecular determinants of their specificity. Spectroscopic measurements reveal differences in copper co-ordination upon the binding of xylan and glucans. LsAA9A activity is less sensitive to the reducing agent potential when cleaving xylan, suggesting that distinct catalytic mechanisms exist for xylan and glucan cleavage. Overall, these data show that AA9 LPMOs can display different apparent substrate specificities dependent upon both productive protein–carbohydrate interactions across a binding surface and also electronic considerations at the copper active site., Copper-dependent lytic polysaccharide monooxygenases (LPMOs) oxidatively cleave polysaccharides. Here the authors present a structure-function characterization of fungal LPMOs, showing that a particular LPMO cleaves xylan using a mechanism that involves an alternative copper coordination geometry.

Published
2017

4. Combined effect of copper and hydrodynamic conditions on Myriophyllum alterniflorum biomarkers

Author

Patrice Fondanèche, Véronique Kazpard, Maha Krayem, Pascal Labrousse, Véronique Deluchat, Philippe Hourdin, Florence Lecavelier Des Etangs, Christian Moesch, Groupement de Recherche Eau, Sol, Environnement (GRESE), Université de Limoges (UNILIM), Service de Pharmacologie, toxicologie et pharmacovigilance [CHU Limoges], CHU Limoges, Lebanese University [Beirut] (LU), Neuroépidémiologie Tropicale (NET), CHU Limoges-Institut d'Epidémiologie Neurologique et de Neurologie Tropicale-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST), and Université de Limoges (UNILIM)-Université de Limoges (UNILIM)

Subjects
0106 biological sciences, Chlorophyll, Health, Toxicology and Mutagenesis, MESH: Plant Shoots, MESH: Plant Roots, MESH: Water Quality, 010501 environmental sciences, 01 natural sciences, MESH: Chlorophyll A, Plant Roots, chemistry.chemical_compound, Water Quality, Biomonitoring, Osmotic pressure, Photosynthesis, MESH: Photosynthesis, biology, General Medicine, Pollution, 6. Clean water, MESH: Copper, Environmental chemistry, Shoot, MESH: Hydrogen Peroxide, MESH: Chlorophyll, MESH: Environmental Monitoring, Plant Shoots, Environmental Monitoring, Chlorophyll a, Environmental Engineering, Cell Respiration, chemistry.chemical_element, Myriophyllum alterniflorum, MESH: Hydrodynamics, Aquatic plant, Environmental Chemistry, 0105 earth and related environmental sciences, Chlorophyll A, Public Health, Environmental and Occupational Health, General Chemistry, Hydrogen Peroxide, biology.organism_classification, Copper, Hydrodynamic conditions, chemistry, Oxidative stress, MESH: Biomarkers, Hydrodynamics, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, MESH: Cell Respiration, Biomarkers, 010606 plant biology & botany
Abstract

The aim of this study is to determine the combined effect of copper and hydrodynamic conditions on the response of certain biomarkers of an aquatic macrophyte, namely Myriophyllum alterniflorum . Watermilfoil biomarkers are monitored in a synthetic medium enriched or not with copper (100 μg.L −1 ) for 21 days in aquarium systems (150 L), under three hydrodynamic conditions: laminar, turbulent, and calm. The studied biomarkers are: respiratory and photosynthetic activities; concentrations of chlorophyll a , b and carotenoids; osmotic potential; hydrogen peroxide content; and growth. In addition, Cu contents in water and in Myriophyllum alterniflorum (roots and shoots) are investigated. The hydrodynamic conditions only affect watermilfoil morphology. Copper accumulates less in turbulent zones; moreover, it is more likely to accumulate in shoots than in roots, except within the calm zone. Cu leads to: i) a significant increase in H 2 O 2 content, ii) a decrease in root growth, pigment content, osmotic potential, photosynthesis and respiration rates, and iii) an inhibition of shoot branching. Differential effects are also observed between younger and older parts, thus indicating the benefit of considering these two plant parts separately in water quality biomonitoring.

Published
2017

5. Structural and Electronic Snapshots during the Transition from a Cu(II) to Cu(I) Metal Center of a Lytic Polysaccharide Monooxygenase by X-ray Photoreduction

Author

Jerry Ståhlberg, Gustav Vaaje-Kolstad, Antoine Royant, Gregg T. Beckham, Daniel Lundberg, Seonah Kim, Majid Hadadd Momeni, Vincent G. H. Eijsink, Mats Sandgren, Takuya Ishida, Miao Wu, Mikael Gudmundsson, Department of Physics, Stockholm University, Institut de biologie structurale (IBS - UMR 5075 ), 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)-Centre National de la Recherche Scientifique (CNRS), University of Luebeck, Biotechnology and Food Science (Department of Chemistry), Center for Molecular Microbiology, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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)

Subjects
inorganic chemicals, Models, Molecular, MESH: Oxidation-Reduction, MESH: Databases, Protein, MESH: Enterococcus faecalis, Inorganic chemistry, MESH: Catalytic Domain, Electrons, Crystal structure, Biochemistry, Mixed Function Oxygenases, Metal, MESH: X-Rays, Polysaccharides, Oxidation state, Catalytic Domain, Enterococcus faecalis, Molecule, Databases, Protein, Molecular Biology, MESH: Electrons, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, Chemistry, X-Rays, Active site, Cell Biology, MESH: Mixed Function Oxygenases, Photochemical Processes, Oxygen, MESH: Copper, Crystallography, Trigonal bipyramidal molecular geometry, MESH: Polysaccharides, visual_art, X-ray crystallography, Enzymology, biology.protein, visual_art.visual_art_medium, Quantum Theory, MESH: Photochemical Processes, Oxidation-Reduction, MESH: Quantum Theory, Copper, MESH: Oxygen, MESH: Models, Molecular
Abstract

International audience; Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes that employ a copper-mediated, oxidative mechanism to cleave glycosidic bonds. The LPMO catalytic mechanism likely requires that molecular oxygen first binds to Cu(I), but the oxidation state in many reported LPMO structures is ambiguous, and the changes in the LPMO active site required to accommodate both oxidation states of copper have not been fully elucidated. Here, a diffraction data collection strategy minimizing the deposited x-ray dose was used to solve the crystal structure of a chitin-specific LPMO from Enterococcus faecalis (EfaCBM33A) in the Cu(II)-bound form. Subsequently, the crystalline protein was photoreduced in the x-ray beam, which revealed structural changes associated with the conversion from the initial Cu(II)-oxidized form with two coordinated water molecules, which adopts a trigonal bipyramidal geometry, to a reduced Cu(I) form in a T-shaped geometry with no coordinated water molecules. A comprehensive survey of Cu(II) and Cu(I) structures in the Cambridge Structural Database unambiguously shows that the geometries observed in the least and most reduced structures reflect binding of Cu(II) and Cu(I), respectively. Quantum mechanical calculations of the oxidized and reduced active sites reveal little change in the electronic structure of the active site measured by the active site partial charges. Together with a previous theoretical investigation of a fungal LPMO, this suggests significant functional plasticity in LPMO active sites. Overall, this study provides molecular snapshots along the reduction process to activate the LPMO catalytic machinery and provides a general method for solving LPMO structures in both copper oxidation states.

Published
2014

6. Antioxidant, metal-binding and DNA-damaging properties of flavonolignans: A joint experimental and computational highlight based on 7-O-galloylsilybin

Author

Veronika Nezhodová, Vladimír Křen, Patrick Trouillas, Jan Hrbac, Jitka Ulrichová, Thomas Desmier, Martina Zatloukalová, Jan Vacek, Martin Kubala, Centre of Biocatalysis and Biotransformation, Institute of Microbiology, Czech Academy of Sciences [Prague] (CAS), Pharmacologie des Immunosuppresseurs et de la Transplantation (PIST), Université de Limoges (UNILIM)-CHU Limoges-Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503)-Institut National de la Santé et de la Recherche Médicale (INSERM), and Marquet, Pierre

Subjects
Antioxidant, DNA damage, DPPH, Stereochemistry, medicine.medical_treatment, Molecular Dynamics Simulation, 010402 general chemistry, Toxicology, 01 natural sciences, Antioxidants, Metal, Flavonolignans, chemistry.chemical_compound, Picrates, MESH: Spectrophotometry, Ultraviolet, medicine, Flavonolignan, Moiety, MESH: Molecular Dynamics Simulation, MESH: DNA Damage, MESH: Picrates, 010405 organic chemistry, Biphenyl Compounds, MESH: Antioxidants, Electrochemical Techniques, General Medicine, [SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences, MESH: Electrochemical Techniques, 0104 chemical sciences, [SDV.SP] Life Sciences [q-bio]/Pharmaceutical sciences, MESH: Copper, MESH: Luminescent Measurements, chemistry, Polyphenol, visual_art, Luminescent Measurements, visual_art.visual_art_medium, Spectrophotometry, Ultraviolet, Copper, MESH: Biphenyl Compounds, DNA Damage, Silymarin, MESH: Silymarin
Abstract

International audience; Besides the well-known chemoprotective effects of polyphenols, their prooxidant activities via interactions with biomacromolecules as DNA and proteins are of the utmost importance. Current research focuses not only on natural polyphenols but also on synthetically prepared analogs with promising biological activities. In the present study, the antioxidant and prooxidant properties of a semi-synthetic flavonolignan 7-O-galloylsilybin (7-GSB) are described. The presence of the galloyl moiety significantly enhances the antioxidant capacity of 7-GSB compared to that of silybin (SB). These findings were supported by electrochemistry, DPPH (2,2-diphenyl-1-picrylhydrazyl) scavenging activity, total antioxidant capacity (CL-TAC) and DFT (density functional theory) calculations. A three-step oxidation mechanism of 7-GSB is proposed at pH 7.4, in which the galloyl moiety is first oxidized at Ep,1=+0.20V (vs. Ag/AgCl3M KCl) followed by oxidation of the 20-OH (Ep,2=+0.55V) and most probably 5-OH (Ep,3=+0.95V) group of SB moiety. The molecular orbital analysis and the calculation of O-H bond dissociation enthalpies (BDE) fully rationalize the electrooxidation processes. The metal (Cu(2+)) complexation of 7-GSB was studied, which appeared to involve both the galloyl moiety and the 5-OH group. The prooxidant effects of the metal-complexes were then studied according to their capacity to oxidatively induce DNA modification and cleavage. These results paved the way towards the conclusion that 7-O-galloyl substitution to SB concomitantly (i) enhances antioxidant (ROS scavenging) capacity and (ii) decreases prooxidant effect/DNA damage after Cu complexation. This multidisciplinary approach provides a comprehensive mechanistic picture of the antioxidant vs. metal-induced prooxidant effects of flavonolignans at the molecular level, under ex vivo conditions.

Published
2013

7. Adaptation of genetically monomorphic bacteria: evolution of copper resistance through multiple horizontal gene transfers of complex and versatile mobile genetic elements

Author

Aude Chabirand, Christian Vernière, Pierre Lefeuvre, Olivier Pruvost, Claudine Boyer, Pierre Grygiel, Damien Richard, Virginie Ravigné, Adrien Rieux, Marie Annabelle Terville, Isabelle Robène, B.I. Canteros, Stéphanie Javegny, Benoit Facon, Karine Boyer, Peuplements végétaux et bioagresseurs en milieu tropical (UMR PVBMT), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut de Recherche pour le Développement (IRD)-Institut National de la Recherche Agronomique (INRA)-Université de La Réunion (UR), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad), Agence nationale de sécurité sanitaire de l'alimentation, de l'environnement et du travail (ANSES), Centre de Biologie pour la Gestion des Populations (UMR CBGP), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut de Recherche pour le Développement (IRD [France-Sud])-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut National de la Recherche Agronomique (INRA), Instituto Nacional de Tecnología Agropecuaria (INTA), Biologie et Génétique des Interactions Plante-Parasite (UMR BGPI), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA), European Regional Development Fund (ERDF), European Agricultural Fund for Rural Development (EAFRD), Conseil Departemental de la Reunion, Region Reunion, Etat francais, French Agropolis Foundation (Labex Agro - Montpellier, E-SPACE) : 1504-004, ANSES, CIRAD, Département Systèmes Biologiques (Cirad-BIOS), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro), The European Regional Development Fund (ERDF) and European Agricultural Fund for Rural Development (EAFRD), Conseil Departemental de la Reunion, Region Reunion, Etat francais, the French Agropolis Foundation (Labex Agro - Montpellier, E-SPACE project number 1504-004), ANSES and CIRAD provided financial support., ANR-10-LABX-0001,AGRO,Agricultural Sciences for sustainable Development(2010), and Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)

Subjects
0301 basic medicine, Citrus, heavy metal resistance, Xanthomonas campestris citri, Xanthomonas citri, Plasmid, Genetics, biology, Adaptation, Physiological, Épidémiologie, MESH: Copper, Stenotrophomonas, PCR, Organisme génétiquement modifié, Cuivre, Citrus canker, mobile DNA, Martinique, MESH: Interspersed Repetitive Sequences, résistance aux maladies, DNA, Bacterial, Séquence nucléotidique, Xanthomonas, Gene Transfer, Horizontal, Genotype, Argentina, Bacterial genome size, MESH: Xanthomonas, 03 medical and health sciences, stomatognathic system, plasmid, MESH: Drug Resistance, Bacterial, Drug Resistance, Bacterial, protection des plantes, contemporary adaptation, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Adaptation, Ecology, Evolution, Behavior and Systematics, H20 - Maladies des plantes, Plant Diseases, Résistance aux pesticides, amélioration génétique, Résistance aux produits chimiques, Xanthomonadaceae, Biologie moléculaire, Microsatellite, biology.organism_classification, Interspersed Repetitive Sequences, resistance to diseases, 030104 developmental biology, Genetics, Population, Gène, Genes, Bacterial, Évaluation, U30 - Méthodes de recherche, Mobile genetic elements, Reunion, Copper, crop protection, Microsatellite Repeats
Abstract

Copper-based compounds are widely used in integrated pest management (1PM) programs aiming at controlling agriculturally important plant bacterial pathogens and the latter have adapted in response to this selective pressure. Copper resistance of Xanthomonas citri pv. citri (Xcc), a major citrus pathogen worldwide causing Asialie citrus canker, was first observed in Argentina two decades ago and subsequently reported as a copLAB-based, plasmid-encoded system. The emergence of resistant strains has since been reported in Réunion (South West lndian Ocean) and Martinique (Eastern Caribbean Sea). Disease severity was found markedly increased in groves established with susceptible cultivars and infected with copper-resistant Xcc. Using tandem repeat-based genotyping and copLAB PCR, we demonstrated that the genetic structure of the copperresistant strains from these three regions was made up of two distant clusters and varied for the detection of copLAB amplicons. ln order to investigate this pattern more closely, we sequenced six copper-resistant Xcc strains from Argentina, Martinique and Réunion, together with reference copper-resistant Xanthomonas and Stenotrophomonas strains using long-read sequencing technology. Genes involved in copper resistance were found to be strain-dependent with the nove! identification in Xcc of copABCD and a eus heavy metal efflux resistance-nodulation-division system. The genes providing the adaptive trait were part of a mobile genetic element similar to Tn3-like transposons and included in a conjugative plasmid. The mining of ail bacterial genomes available from public databases suggested that the mobile elements containing copper resistance genes and their plasmid environments were primarily detected in the Xanthomonadaceae family.

Published
2016

8. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes

Author

Paul A. Cobine, Dennis R. Winge, Fabien Pierrel, University of Utah, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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)

Subjects
Models, Molecular, Protein Conformation, MESH: Mitochondria, Mitochondrial intermembrane space, MESH: Biological Transport, chemistry.chemical_element, macromolecular substances, Mitochondrion, Cytochrome oxidase, Electron Transport Complex IV, Superoxide dismutase, 03 medical and health sciences, MESH: Protein Conformation, MESH: Electron Transport Complex IV, COX17, Cytochrome c oxidase, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, 030304 developmental biology, 0303 health sciences, biology, Chemistry, Metallochaperone, 030302 biochemistry & molecular biology, nutritional and metabolic diseases, Biological Transport, Cell Biology, Copper, Mitochondria, MESH: Copper, Biochemistry, Cytoplasm, Mitochondrial matrix, Biophysics, biology.protein, MESH: Models, Molecular
Abstract

International audience; Copper is required within the mitochondrion for the function of two metalloenzymes, cytochrome c oxidase (CcO) and superoxide dismutase (Sod1). Copper metallation of these two enzymes occurs within the mitochondrial intermembrane space and is mediated by metallochaperone proteins. Cox17 is a key copper donor to two accessory proteins, Sco1 and Cox11, to form the two copper centers in the mature CcO complex. Ccs1 is the necessary metallochaperone for the copper metallation of Sod1 in the IMS as well as within the cytoplasm where the bulk of Sod1 resides. Copper ions used in the metallation of CcO and Sod1 appear to be provided by a novel copper pool within the mitochondrial matrix. This review documents copper ion shuttling within the mitochondrion and the proteins that mediate assembly of active CcO and Sod1.

Published
2006

9. Characterization of a UDP-N-acetyl-<scp>D</scp>-galactosamine:polypeptide N-acetylgalactosaminyltransferase with an unusual lectin domain from the platyhelminth parasite Echinococcus granulosus

Author

Teresa Freire, Cora Chalar, Carlos Robello, Pedro M. Alzari, Cecilia Fernández, Eduardo Osinaga, Rick M. Maizels, Facultad de Medicina [Universidad de la Republica, Uruguay], Universidad de la República [Montevideo] (UCUR), University of Edinburgh, Facultad de Ciencias (UDELAR), Biochimie Structurale, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], This work was supported in part by Comisión Sectorial de Investigación Científica (Uruguay) and the ECOS France–Uruguay Programme. C.F. was awarded a Travel Research Fellowship from the Wellcome Trust., Universidad de la República [Montevideo] (UDELAR), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Sequence Analysis, DNA, MESH: Hydrogen-Ion Concentration, MESH: Helminth Proteins, Helminth genetics, MESH: Amino Acid Sequence, MESH: DNA, Helminth, MESH: Echinococcus granulosus, Biochemistry, Substrate Specificity, MESH: Protein Structure, Tertiary, chemistry.chemical_compound, MESH: Lectins, Protein structure, MESH: Chlorocebus aethiops, Lectins, Chlorocebus aethiops, MESH: Cattle Diseases, MESH: Animals, Cloning, Molecular, Echinococcus granulosus, Peptide sequence, O-glycosylation, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], biology, MESH: Peptides, 030302 biochemistry & molecular biology, Helminth Proteins, DNA, Helminth, Hydrogen-Ion Concentration, MESH: COS Cells, MESH: Copper, MESH: Cattle, Transmembrane domain, COS Cells, N-Acetylgalactosaminyltransferases, Research Article, DNA, Complementary, UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, Glycosylation, [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph], Molecular Sequence Data, Polypeptide N-acetylgalactosaminyltransferase, Cattle Diseases, MESH: Manganese, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, MESH: N-Acetylgalactosaminyltransferases, helminth parasite, Cell Line, MESH: Echinococcosis, 03 medical and health sciences, Echinococcosis, parasitic diseases, [CHIM.CRIS]Chemical Sciences/Cristallography, Animals, MESH: Cloning, Molecular, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, Manganese, MESH: Molecular Sequence Data, Lectin, Sequence Analysis, DNA, MESH: DNA, Complementary, Cell Biology, biology.organism_classification, Protein Structure, Tertiary, MESH: Cell Line, chemistry, biology.protein, Cattle, MESH: Substrate Specificity, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Peptides, Copper
Abstract

International audience; As part of a general project aimed at elucidating the initiation of mucin-type O-glycosylation in helminth parasites, we have characterized a novel ppGalNAc-T (UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase) from the cestode Echinococcus granulosus (Eg-ppGalNAc-T1). A full-length cDNA was isolated from a library of the tissue-dwelling larval stage of the parasite, and found to code for a 654-amino-acid protein containing all the structural features of ppGalNAc-Ts. Functional characterization of a recombinant protein lacking the transmembrane domain showed maximal activity at 28 degrees C, in the range 6.5-7.5 pH units and in the presence of Cu2+. In addition, it transferred GalNAc to a broad range of substrate peptides, derived from human mucins and O-glycosylated parasite proteins, including acceptors containing only serine or only threonine residues. Interestingly, the C-terminal region of Eg-ppGalNAc-T1 bears a highly unusual lectin domain, considerably longer than the one from other members of the family, and including only one of the three ricin B repeats generally present in ppGalNAc-Ts. Furthermore, a search for conserved domains within the protein C-terminus identified a fragment showing similarity to a recently defined domain, specialized in the binding of organic phosphates (CYTH). The role of the lectin domain in the determination of the substrate specificity of these enzymes suggests that Eg-ppGalNAc-T1 would be involved in the glycosylation of a special type of substrate. Analysis of the tissue distribution by in situ hybridization and immunohistochemistry revealed that this transferase is expressed in the hydatid cyst wall and the subtegumental region of larval worms. Therefore it could participate in the biosynthesis of O-glycosylated parasite proteins exposed at the interface between E. granulosus and its hosts.

Published
2004

10. Transcriptomic and metabolomic analysis of copper stress acclimation in Ectocarpus siliculosus highlights signaling and tolerance mechanisms in brown algae

Author

Sophie Goulitquer, Andrés Ritter, Juan A. Correa, Thierry Tonon, Catherine Boyen, Simon M. Dittami, Philippe Potin, Departamento de Ecología Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile (UC), Végétaux marins et biomolécules, Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-GOEMAR-Centre National de la Recherche Scientifique (CNRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Departamento de Ecologia, Departamento de Ecología, Facultad de Ciencias Biologicas, Pontificia Universidad Catolica de Chile, Santiago, Chile, Departamento de Ecología, Facultad de Ciencias Biologicas, Pontificia Universidad Catolica de Chile, Santiago, Chile-Departamento de Ecología, Facultad de Ciencias Biologicas, Pontificia Universidad Catolica de Chile, Santiago, Chile, Center of applied ecology & sustainability (CAPES), Facultad de ciencias biologicas [Santiago], Pontificia Universidad Católica de Chile (UC)-Pontificia Universidad Católica de Chile (UC), Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Défense des algues, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Station biologique de Roscoff [Roscoff] (SBR), MetaboMER, Université Pierre et Marie Curie - Paris 6 (UPMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)-Station biologique de Roscoff [Roscoff] (SBR)

Subjects
MESH: Signal Transduction, MESH: Algal Proteins, MESH: Amino Acids, Acclimatization, Molecular Networks (q-bio.MN), [SDV]Life Sciences [q-bio], Primary metabolism, Plant Science, medicine.disease_cause, MESH: Down-Regulation, MESH: Least-Squares Analysis, MESH: Up-Regulation, Cluster Analysis, Quantitative Biology - Molecular Networks, Amino Acids, Photosynthesis, MESH: Metabolomics, MESH: Phylogeny, MESH: Stress, Physiological, Chromatography, High Pressure Liquid, Phylogeny, MESH: Photosynthesis, [SDU.OCEAN]Sciences of the Universe [physics]/Ocean, Atmosphere, Abiotic component, Copper stress response, MESH: Oxidative Stress, Ectocarpus siliculosus, Fatty Acids, Discriminant Analysis, MESH: Phaeophyta, Up-Regulation, MESH: Fatty Acids, Cell biology, MESH: Copper, Heavy metal, ABC transporters, Metabolome, Metabolic Networks and Pathways, MESH: Metabolome, Research Article, Signal Transduction, MESH: Oxylipins, Brown algae, Down-Regulation, MESH: Acclimatization, Biology, Phaeophyta, Gas Chromatography-Mass Spectrometry, MESH: Gene Expression Profiling, Metabolomics, Stress, Physiological, Botany, medicine, Humans, Quantitative Biology - Genomics, Oxylipins, 14. Life underwater, Least-Squares Analysis, MESH: Chromatography, High Pressure Liquid, Genomics (q-bio.GN), MESH: Humans, Abiotic stress, Gene Expression Profiling, MESH: Transcriptome, Algal Proteins, MESH: Discriminant Analysis, Oxylipin, biology.organism_classification, MESH: Cluster Analysis, MESH: Gas Chromatography-Mass Spectrometry, Oxidative Stress, Multicellular organism, MESH: Metabolic Networks and Pathways, FOS: Biological sciences, Transcriptome, Copper, Oxidative stress
Abstract

International audience; Background: Brown algae are sessile macro-organisms of great ecological relevance in coastal ecosystems. They evolved independently from land plants and other multicellular lineages, and therefore hold several original ontogenic and metabolic features. Most brown algae grow along the coastal zone where they face frequent environmental changes, including exposure to toxic levels of heavy metals such as copper (Cu). Results: We carried out large-scale transcriptomic and metabolomic analyses to decipher the short-term acclimation of the brown algal model E. siliculosus to Cu stress, and compared these data to results known for other abiotic stressors. This comparison demonstrates that Cu induces oxidative stress in E. siliculosus as illustrated by the transcriptomic overlap between Cu and H 2 O 2 treatments. The common response to Cu and H 2 O 2 consisted in the activation of the oxylipin and the repression of inositol signaling pathways, together with the regulation of genes coding for several transcription-associated proteins. Concomitantly, Cu stress specifically activated a set of genes coding for orthologs of ABC transporters, a P 1B-type ATPase, ROS detoxification systems such as a vanadium-dependent bromoperoxidase, and induced an increase of free fatty acid contents. Finally we observed, as a common abiotic stress mechanism, the activation of autophagic processes on one hand and the repression of genes involved in nitrogen assimilation on the other hand. Conclusions: Comparisons with data from green plants indicate that some processes involved in Cu and oxidative stress response are conserved across these two distant lineages. At the same time the high number of yet uncharacterized brown alga-specific genes induced in response to copper stress underlines the potential to discover new components and molecular interactions unique to these organisms. Of particular interest for future research is the potential cross-talk between reactive oxygen species (ROS)-, myo-inositol-, and oxylipin signaling.

Published
2014

11. Joint-action of antifouling substances in copper-free paints

Author

Karine Vallée-Réhel, David Carteau, Isabelle Linossier, Maxime Delbury, Fabienne Faÿ, Laboratoire de Biotechnologie et Chimie Marines (LBCM), Université de Bretagne Sud (UBS)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), and Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Non ionic, Biofouling, chemistry.chemical_element, Polysorbates, 02 engineering and technology, MESH: Paint, Toxicology, 03 medical and health sciences, chemistry.chemical_compound, Colloid and Surface Chemistry, Paint, Zinc peroxide, Physical and Theoretical Chemistry, Hydrogen peroxide, 0303 health sciences, 030306 microbiology, Chlorhexidine, MESH: Polysorbates, Eukaryota, Surfaces and Interfaces, General Medicine, Hydrogen Peroxide, MESH: Biofouling, 021001 nanoscience & nanotechnology, Copper, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Joint action, MESH: Chlorhexidine, MESH: Copper, MESH: Eukaryota, chemistry, Chemical engineering, Tributyltin, MESH: Hydrogen Peroxide, 0210 nano-technology, Biotechnology
Abstract

International audience; Due to the environmentally harmful impact of tributyltin self-polishing paints, there is a critical need of more ecological alternatives. The aim of the present work is to study the joint-action of three molecules chosen in order to combine the two modes of prevention: chemical and physical repelling of biofouling. This "hybrid" system is principally dedicated to disturb durable settlement of microfouling. Each component was chosen according to its specific properties: chlorhexidine is a bisdiguanide antiseptic with antibacterial activity, zinc peroxide is an inorganic precursor of high instable entities which react with seawater to create hydrogen peroxide, Tween 85 is a non ionic surfactant disturbing interactions between colonizing organisms and surface. Obtained results highlighted the interest on mixing such molecules to get additive action on antifouling efficiency.

Published
2012

12. PtrA is a periplasmic protein involved in Cu tolerance in Pseudomonas aeruginosa

Author

Michel Ragno, Ina Attree, Sylvie Elsen, 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), Pathogénie bactérienne et réponses cellulaires, and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Transcription, Genetic, chemistry.chemical_element, medicine.disease_cause, Microbiology, Type three secretion system, Periplasmic Proteins, 03 medical and health sciences, Bacterial Proteins, Drug Resistance, Bacterial, MESH: Drug Resistance, Bacterial, medicine, Molecular Biology, MESH: Bacterial Proteins, 030304 developmental biology, Molecular Biology of Pathogens, 0303 health sciences, MESH: Gene Expression Regulation, Bacterial, biology, 030306 microbiology, Pseudomonas aeruginosa, MESH: Transcription, Genetic, Gene Expression Regulation, Bacterial, Periplasmic space, biology.organism_classification, Copper, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Copper, Biochemistry, chemistry, Pseudomonadales, MESH: Pseudomonas aeruginosa, Bacteria, Pseudomonadaceae, MESH: Periplasmic Proteins
Abstract

In this work, we demonstrate that PtrA (U. H. Ha et al., Mol. Microbiol. 54:307–320, 2004) is a periplasmic protein, specifically synthesized in the presence of copper, that is involved in the tolerance of Pseudomonas aeruginosa to copper. Our biochemical and genetic analyses challenge its role in transcriptional inhibition of the type III secretion system.

Published
2011

13. Effects of copper on the photosynthesis of intact chloroplasts: interaction with manganese

Author

Mário Pádua, Serge Aubert, Richard Bligny, Adalcina Casimiro, Ana M. Cavaco, Escola Superior de Tecnologia da Saude de Lisboa, Centro de Electronica, Optoelectronica e Telecomunicaçoes [Faro] (CEOT), Universidade do Algarve (UAlg), Station alpine Joseph Fourier - UMS 3370 (SAJF), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Departamento de Biologia Vegetal, Faculdade de Ciencias da Universidade de Lisboa, Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
Chlorophyll, 0106 biological sciences, Chloroplasts, Photoinhibition, photosynthesis inhibition, Photosystem II, Physiology, plant, Plant Science, Photochemistry, MESH: Carbon Dioxide, 01 natural sciences, Chloroplast membrane, stress, Spinacia oleracea, MESH: Oxygen Consumption, Photosynthesis, Chlorophyll fluorescence, MESH: Photosynthesis, 0303 health sciences, MESH: Spinacia oleracea, MESH: Photosystem II Protein Complex, food and beverages, General Medicine, Chloroplast, MESH: Copper, Thylakoid, manganese, MESH: Chlorophyll, chemistry.chemical_element, MESH: Manganese, MESH: Peas, Fluorescence, 03 medical and health sciences, Oxygen Consumption, chloroplast, Genetics, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, Manganese, MESH: Chloroplasts, MESH: Fluorescence, Peas, Photosystem II Protein Complex, Cell Biology, Carbon Dioxide, heavy metal, Copper, chemistry, copper, metabolism, 010606 plant biology & botany
Abstract

International audience; Highly purified, intact chloroplasts were prepared from pea (Pisum sativum L.) and spinach (Spinacia oleracea L.) following an identical procedure, and were used to investigate the cupric cation inhibition on the photosynthetic activity. In both species, copper inhibition showed a similar inhibitor concentration that decreases the enzyme activity by 50% (IC(50) approximately 1.8 microM) and did not depend on the internal or external phosphate (Pi) concentration, indicating that copper did not interact with the Pi translocator. Fluorescence analysis suggested that the presence of copper did not facilitate photoinhibition, because there were no changes in maximal fluorescence (F(m)) nor in basal fluorescence (F(o)) of copper-treated samples. The electron transport through the photosystem II (PSII) was also not affected (operating efficiency of PSII-F'v/F'm similar in all conditions). Yet, under Cu(2+) stress, the proportion of open PSII reaction centers was dramatically decreased, and the first quinone acceptor (Q(A)) reoxidation was fully inhibited, as demonstrated by the constant photochemical quenching (q(P)) along experiment time. The quantum yield of PSII electron transport (Phi(PSII)) was also clearly affected by copper, and therefore reduced the photochemistry efficiency. Manganese, when added simultaneously with copper, delayed the inhibition, as measured by oxygen evolution and chlorophyll fluorescence, but neither reversed the copper effect when added to copper-inhibited plastids, nor prevented the inhibition of the Hill activity of isolated copper-treated thylakoids. Our results suggest that manganese competed with copper to penetrate the chloroplast envelope. This competition seems to be specific because other divalent cations e.g. magnesium and calcium, did not interfere with the copper action in intact chloroplasts. All results do suggest that, under these conditions, the stroma proteins, such as the Calvin-Benson cycle enzymes or others are the most probable first target for the Cu(2+) action, resulting in the total inhibition of chloroplast photosynthesis and in the consequent unbalanced rate of production and consumption of the reducing power.

Published
2010

14. Iron excess treatable by copper supplementation in acquired aceruloplasminemia: a new form of secondary human iron overload?

Author

Marie-Bérengère Troadec, Dorothée Videt-Gibou, Edouard Bardou-Jacquet, Serge Belliard, Joseph Rivalan, Olivier Loréal, Caroline Le Lan, Anne-Marie Jouanolle, Pierre Brissot, Service de neurologie [Rennes], Université de Rennes (UR), Régulations des équilibres fonctionnels du foie normal et pathologique, Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de génétique moléculaire et génomique médicale [CHU Rennes], CHU Pontchaillou [Rennes], Service de néphrologie [Rennes], Université de Rennes (UR)-Hôpital Pontchaillou-CHU Pontchaillou [Rennes], Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de génétique moléculaire, Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CHU Pontchaillou [Rennes], Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Hôpital Pontchaillou-CHU Pontchaillou [Rennes], and Le Corre, Morgane

Subjects
medicine.medical_specialty, 030309 nutrition & dietetics, Immunology, MESH: Metal Metabolism, Inborn Errors, Iron overload disorder, chemistry.chemical_element, MESH: Dietary Supplements, Biochemistry, 03 medical and health sciences, MESH: Iron Overload, Internal medicine, medicine, CERULOPLASMIN DEFICIENCY, Aceruloplasminemia, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, MESH: Humans, MESH: Middle Aged, biology, [SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, Cell Biology, Hematology, medicine.disease, Copper, [SDV.MHEP.HEG] Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, MESH: Male, MESH: Copper, Endocrinology, chemistry, biology.protein, Ceruloplasmin
Abstract

To the editor: Ceruloplasmin plays a major role in iron mobilization from the tissues stores through its ferroxidase activity.[1][1],[2][2] Hereditary aceruloplasminemia is an autosomal recessive iron overload disorder resulting from mutations in the ceruloplasmin gene.[3][3],[4][4] Acquired

Published
2009

15. Subgram daily supplementation with docosahexaenoic acid protects low-density lipoproteins from oxidation in healthy men

Author

Michel Lagarde, Evelyne Véricel, Michel Guichardant, Nicolas Guillot, Catherine Calzada, Romain A. Colas, Martine Laville, Régulations métaboliques, nutrition et diabètes - UM55 (RMND UM55), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de la Recherche Agronomique (INRA), Centre de Recherche en Nutrition Humaine Rhône-Alpes (CRNH-RA), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Recherche Agronomique (INRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Jean Monnet [Saint-Étienne] (UJM)-CHU Saint-Etienne-Hospices Civils de Lyon (HCL)-CHU Grenoble, Agence Nationale de la Recherche (ANR) 2005 'Cardiovasculaire, Obésité et Diabète', Groupe Lipides et Nutrition (GLN) and Agence Nationale de la Recherche (ANR) 2005 'Cardiovasculaire, Obésité et Diabète'., Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche en Nutrition Humaine Rhône-Alpes (CRNH-RH), Université de Lyon-Université de Lyon-Institut National de la Recherche Agronomique (INRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Jean Monnet [Saint-Étienne] (UJM)-CHU Saint-Etienne-Hospices Civils de Lyon (HCL)-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Agence Nationale de la Recherche (ANR) 2005 'Cardiovasculaire, Obésité et Diabète',Agence Nationale de la Recherche (ANR) 2005 'Cardiovasculaire, Obésité et Diabète', Cardiovasculaire, métabolisme, diabétologie et nutrition (CarMeN), Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National de la Recherche Agronomique (INRA), Université de Lyon-Université de Lyon-CHU Grenoble-Hospices Civils de Lyon (HCL)-CHU Saint-Etienne-Université Jean Monnet - Saint-Étienne (UJM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Vericel, Evelyne, and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Male, n-3 Polyunsaturated fatty acids Antioxidant Peroxidation Low-density lipoproteins, MESH: Lipoproteins, LDL, 030309 nutrition & dietetics, [SDV]Life Sciences [q-bio], alpha-Tocopherol, MESH: Dietary Supplements, MESH: Lipid Peroxidation, Antioxidants, Lipid peroxidation, Cohort Studies, chemistry.chemical_compound, MESH: Vitamin E, Malondialdehyde, Vitamin E, MESH: Cohort Studies, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, MESH: Aged, 0303 health sciences, MESH: Middle Aged, Fatty Acids, food and beverages, MESH: Fatty Acids, Unsaturated, Middle Aged, Eicosapentaenoic acid, 3. Good health, MESH: Fatty Acids, MESH: Copper, Lipoproteins, LDL, MESH: Docosahexaenoic Acids, Biochemistry, MESH: alpha-Tocopherol, Docosahexaenoic acid, Low-density lipoprotein, Fatty Acids, Unsaturated, lipids (amino acids, peptides, and proteins), Cardiology and Cardiovascular Medicine, MESH: Oxygen, Polyunsaturated fatty acid, medicine.medical_specialty, Docosahexaenoic Acids, MESH: Malondialdehyde, 03 medical and health sciences, Internal medicine, medicine, Humans, Unsaturated fatty acid, 030304 developmental biology, Aged, MESH: Humans, MESH: Antioxidants, MESH: Male, Oxygen, [SDV.AEN] Life Sciences [q-bio]/Food and Nutrition, Endocrinology, chemistry, Dietary Supplements, Lipid Peroxidation, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, Copper, Lipoprotein
Abstract

International audience; OBJECTIVE: To determine the effect of supplementation with increasing doses of docosahexaenoic acid (DHA), as the only n-3 polyunsaturated fatty acid (PUFA), on low-density lipoprotein (LDL) redox status and oxidizability. METHODS: Twelve healthy men aged 53-65 years ingested consecutive doses of DHA (200, 400, 800 and 1600 mg/day), each dose for two weeks. RESULTS: The proportions of DHA increased dose-dependently in LDL phospholipids and cholesteryl esters, even after two weeks of supplementation with 200mg/day DHA. The daily intake of 200, 400 and 800 mg DHA resulted in increased alpha-tocopherol concentrations, decreased MDA concentrations, and a longer lag time for copper-induced LDL oxidation. Supplementation with 1600 mg/day DHA had no effect on the above parameters. In plasma, concentrations of 4-hydroxy-hexenal, specifically derived from the peroxidation of n-3 fatty acids, significantly increased after 800 and 1600 mg DHA, representing 0.01% of plasma n-3 PUFAs, while 4-hydroxy-nonenal concentrations, derived from the peroxidation of n-6 fatty acids, did not change. CONCLUSION: Our results clearly show that an intake of 200-800 mg/day DHA may have protective and antioxidant effects on LDL and could represent optimal doses for cardiovascular disease prevention in a healthy population.

Published
2009

16. X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms

Author

Jacques Covès, Serge Gambarelli, Eric Girard, Antoine P. Maillard, Guillaume Pompidor, Richard Kahn, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-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), Pathogenèse bactérienne et réponses cellulaires (PBRC), 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), 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)-Centre National de la Recherche Scientifique (CNRS), Service de Chimie Inorganique et Biologique (SCIB - UMR E3), Institut Nanosciences et Cryogénie (INAC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), 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 [2016-2019] (UGA [2016-2019])-Institut National de la Santé et de la Recherche Médicale (INSERM)-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)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Metal-sensor, Protein Conformation, [SDV]Life Sciences [q-bio], MESH: Amino Acid Sequence, Signal transduction, Crystallography, X-Ray, 01 natural sciences, Biochemistry, chemistry.chemical_compound, MESH: Apoproteins, MESH: Protein Structure, Tertiary, Protein structure, MESH: Protein Conformation, Structural Biology, Cupriavidus metallidurans CH34, MESH: Bacterial Proteins, 0303 health sciences, biology, Resolution (electron density), Cupriavidus, 3. Good health, MESH: Copper, visual_art, visual_art.visual_art_medium, Periplasmic Proteins, Dimerization, Stereochemistry, Molecular Sequence Data, Biophysics, chemistry.chemical_element, CnrX, 010402 general chemistry, Metal, 03 medical and health sciences, Bacterial Proteins, Genetics, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, MESH: Cupriavidus, MESH: Molecular Sequence Data, Cupriavidus metallidurans, Ligand, Cell Biology, biology.organism_classification, MESH: Crystallography, X-Ray, Copper, 0104 chemical sciences, Protein Structure, Tertiary, Crystallography, chemistry, MESH: Dimerization, X-ray structure, Apoproteins, Derivative (chemistry), Heavy-metal, MESH: Periplasmic Proteins
Abstract

International audience; Both the X-ray structures of the apo- and the copper-bound forms of the metal-sensor domain (residues 31-148) of CnrX from Cupriavidus metallidurans CH34 were obtained at 1.74A resolution from a selenomethionine derivative. This four-helix hooked-hairpin is the first structure of a metal-sensor in an ECF-type signaling pathway. The copper ion is bound in a type 2-like center with a 3N1O coordination in the equatorial plane and shows an unprecedented remote fifth axial ligand with Met93 contributing a weak S-Cu bond. The signal onset cannot be explained by conformational changes associated with CnrX metallation.

Published
2008

17. Cu2+ SPEEDS UP MAUROTOXIN OXIDATIVE FOLDING

Author

Regaya, Imed, Andreotti, Nicolas, Di Luccio, Eric, de Waard, Michel, Sabatier, Jean-Marc, Ingénierie des protéines (IP), Université de la Méditerranée - Aix-Marseille 2-Centre National de la Recherche Scientifique (CNRS), Unité de Protéomie Fonctionnelle & Bioconservation Alimentaire, Institut Supérieur des Sciences Biologiques et Appliquées de Tunis, Canaux calciques , fonctions et pathologies, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was financially supported by the CEA, INSERM, Cellpep S.A. (Paris, France), and CNRS., Collaboration, and Canepari, Marco

Subjects
musculoskeletal diseases, MESH: Oxidation-Reduction, scorpion toxin, [SDV.MHEP.PHY] Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO], MESH: Protein Folding, MESH: Protein Structure, Secondary, MESH: Amino Acid Sequence, Cu2+, MESH: Circular Dichroism, disulphide bridging, MESH: Scorpion Venoms, MESH: Mice, Inbred C57BL, [SDV.MHEP.PHY]Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO], MESH: Animals, MESH: Disulfides, MESH: Mice, mass spectrometry, MESH: Neurotoxins, MESH: Iodoacetamide, MESH: Alkylation, MESH: Molecular Sequence Data, MESH: Copper, maurotoxin, MESH: Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, oxidative folding
Abstract

International audience; Maurotoxin (MTX) is a 34-mer scorpion toxin cross-linked by four disulphide bridges that acts on various K+ channel types. It folds according to an alpha/beta scaffold, i.e., a helix connected to a two stranded beta-sheet by two disulphide bridges. In a former study, various parameters that affect the oxidation and folding of the reduced form of synthetic MTX were investigated in vitro. It was found that MTX achieves its final 3-D structure by evolving over time through a series of oxidation intermediates, from the least to the most oxidized species. MTX oxidative intermediates can be studied by iodoacetamide alkylation of free cysteine residues followed by mass spectrometry analysis. Here, we have analysed the effect of Cu2+ (0.1 to 50 mM) on the kinetics of MTX oxidative folding and found that it dramatically speeds up the formation of the four-disulphide bridged, native-like, MTX (maximal production within 30 minutes instead of > 60 hours). This catalysing effect of Cu2+ was found to be concentration-dependent, reaching a plateau at 10 mM copper ions. Cu2+ was also found to prevent the slow transition of a three disulphide-bridged MTX intermediate towards the final four disulphide-bridged product (12% of total MTX). The data are discussed in light of the potential effects of Cu2+ on MTX secondary structure formation, disulphide bridging and peptidyl prolyl cis-trans isomerization.

Published
2008

18. ATP7B copper-regulated traffic and association with the tight junctions: copper excretion into the bile

Author

Hernandez, Sonia, Tsuchiya, Yo, García-Ruiz, Josefa, Lalioti, Vassiliki, Nielsen, Søren, Cassio, Doris, Sandoval, Ignacio, Centro de Biología Molecular Severo Ochoa [Madrid] (CBMSO), Universidad Autonoma de Madrid (UAM)-Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), The Water and Salt Research Center, Signalisation cellulaire et calcium, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by grants of the Ministerio de Educacion y Ciencia from the Spanish Government (BFU-2005-07903, GEN2003-20662-C07-06) to I.V.S., and Ministerio de Educacion y Ciencia from the Spanish Government (BFU-2005-07903

Subjects
MESH: Humans, MESH: Cell Line, Tumor, MESH: Rats, MESH: Microscopy, Fluorescence, MESH: Rats, Wistar, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, digestive system, MESH: Male, MESH: Hepatocytes, MESH: Copper, MESH: Liver Neoplasms, Experimental, MESH: Cation Transport Proteins, MESH: Antibodies, Neoplasm, MESH: Liver Neoplasms, MESH: Adenosine Triphosphatases, MESH: Blotting, Western, MESH: Animals, MESH: Carcinoma, Hepatocellular, MESH: Bile, MESH: Liver, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; BACKGROUND & AIMS: The copper transporter ATP7B plays a central role in the elimination of excess copper by the liver into the bile, yet the site of its action remains controversial. The studies reported here examine the correspondence between the site of ATP7B action and distribution and the pathways of copper disposal by the liver. METHODS: Microscopy and cell fractionation studies of polarized Can 10 cells forming long-branched bile canaliculi have been used to study the cellular distribution of ATP7B. Copper excretion into the bile was studied in perfused rat liver. RESULTS: Copper excess provokes a massive download of the ATP7B retained in the trans-Golgi network into the bile canalicular membrane. Furthermore, a stable ATP7B pool is localized to the tight junctions that seal the bile canaliculi. The profile of Cu(64) excretion into the bile by isolated rat livers perfused under one-pass conditions provides evidence of copper excretion by 2 separate mechanisms, transcytosis across the hepatocyte and paracellular transport throughout the tight junctions. CONCLUSIONS: Whereas the ATP7B retained in the trans-Golgi-network is massively translocated to the bile canalicular membrane in response to increased copper levels, a pool of ATP7B associated with the tight junctions remains stable. In situ studies indicate that copper is excreted into the bile by 2 separate pathways. The results are discussed in the frame of the normal and impeded excretion of copper into the bile.

Published
2008

19. ATP7B copper-regulated traffic and association with the tight junctions: copper excretion into the bile.: ATP7B and copper excretion by liver

Author

Hernandez, Sonia, Tsuchiya, Yo, García-Ruiz, Josefa, Lalioti, Vassiliki, Nielsen, Søren, Cassio, Doris, Sandoval, Ignacio, Centro de Biología Molecular Severo Ochoa [Madrid] (CBMSO), Universidad Autónoma de Madrid (UAM)-Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), The Water and Salt Research Center, Signalisation cellulaire et calcium, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by grants of the Ministerio de Educacion y Ciencia from the Spanish Government (BFU-2005-07903, GEN2003-20662-C07-06) to I.V.S., Ministerio de Educacion y Ciencia from the Spanish Government (BFU-2005-07903, and U757, .

Subjects
MESH: Humans, MESH: Cell Line, Tumor, MESH: Rats, MESH: Microscopy, Fluorescence, MESH: Rats, Wistar, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, digestive system, MESH: Male, MESH: Hepatocytes, MESH: Copper, MESH: Liver Neoplasms, Experimental, MESH: Cation Transport Proteins, MESH: Antibodies, Neoplasm, MESH: Liver Neoplasms, MESH: Adenosine Triphosphatases, MESH: Blotting, Western, MESH: Animals, MESH: Carcinoma, Hepatocellular, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, MESH: Bile, MESH: Liver, MESH: Electrophoresis, Polyacrylamide Gel
Abstract

International audience; BACKGROUND & AIMS: The copper transporter ATP7B plays a central role in the elimination of excess copper by the liver into the bile, yet the site of its action remains controversial. The studies reported here examine the correspondence between the site of ATP7B action and distribution and the pathways of copper disposal by the liver. METHODS: Microscopy and cell fractionation studies of polarized Can 10 cells forming long-branched bile canaliculi have been used to study the cellular distribution of ATP7B. Copper excretion into the bile was studied in perfused rat liver. RESULTS: Copper excess provokes a massive download of the ATP7B retained in the trans-Golgi network into the bile canalicular membrane. Furthermore, a stable ATP7B pool is localized to the tight junctions that seal the bile canaliculi. The profile of Cu(64) excretion into the bile by isolated rat livers perfused under one-pass conditions provides evidence of copper excretion by 2 separate mechanisms, transcytosis across the hepatocyte and paracellular transport throughout the tight junctions. CONCLUSIONS: Whereas the ATP7B retained in the trans-Golgi-network is massively translocated to the bile canalicular membrane in response to increased copper levels, a pool of ATP7B associated with the tight junctions remains stable. In situ studies indicate that copper is excreted into the bile by 2 separate pathways. The results are discussed in the frame of the normal and impeded excretion of copper into the bile.

Published
2008

20. Cyclic AMP-dependent protein kinase controls energy interconversion during the catalytic cycle of the yeast copper-ATPase

Author

Adalberto Vieyra, Elisabeth Mintz, Rafael H.F. Valverde, Jennifer Lowe, Martine Cuillel, Isabelle Morin, Fisico-Quimica Biologica, Universidade Federal do Rio de Janeiro (UFRJ), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
ATPase, MESH: Catalytic Domain, MESH: Amino Acid Sequence, Biochemistry, MESH: Saccharomyces cerevisiae Proteins, Copper Transport Proteins, Structural Biology, ATP hydrolysis, Catalytic Domain, Serine, Phosphorylation, Cation Transport Proteins, 0303 health sciences, biology, 030302 biochemistry & molecular biology, Copper transport, MESH: Saccharomyces cerevisiae, Transport protein, MESH: Copper, Asparagine, Intracellular, Cell signalling, Saccharomyces cerevisiae Proteins, MESH: Asparagine, MESH: Mutation, Molecular Sequence Data, Biophysics, chemistry.chemical_element, Saccharomyces cerevisiae, Regulatory phosphorylation, Catalysis, 03 medical and health sciences, MESH: Cation Transport Proteins, Genetics, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, MESH: Serine, Protein kinase A, Molecular Biology, 030304 developmental biology, Cyclic AMP-Dependent Protein Kinase Catalytic Subunits, MESH: Molecular Sequence Data, MESH: Phosphorylation, MESH: Cyclic AMP-Dependent Protein Kinase Catalytic Subunits, Cell Biology, MESH: Catalysis, Copper, Yeast, chemistry, Catalytic cycle, Ccc2p, Mutation, biology.protein
Abstract

International audience; The pathogenesis of human Menkes and Wilson diseases depends on alterations in copper transport. Some reports suggest that intracellular traffic of copper might be regulated by kinase-mediated phosphorylation. However, there is no evidence showing the influence of kinase-related processes in coupled ATP hydrolysis/copper transport cycles. Here, we show that cyclic AMP-dependent protein kinase (PKA) regulates Ccc2p, the yeast Cu(I)-ATPase, with PKA-mediated phosphorylation of a conserved serine (Ser258) being crucial for catalysis. Long-range intramolecular communication between Ser258 and Asp627 (at the catalytic site) modulates the key pumping event: the conversion of the high-energy to the low-energy phosphorylated intermediate associated with copper release.

Published
2008

21. Mitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutase

Author

Dennis R. Winge, Fabien Pierrel, Megan Bestwick, Paul A. Cobine, University of Utah, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-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)

Subjects
Glycerol, Cytoplasm, Ligands, Biochemistry, Superoxide Dismutase-1, 0302 clinical medicine, MESH: Saccharomyces cerevisiae Proteins, MESH: Ligands, MESH: Superoxide Dismutase, 0303 health sciences, MESH: Genetic Complementation Test, MESH: Oxidative Stress, biology, Ligand (biochemistry), Mitochondria, MESH: Copper, Phenotype, Mitochondrial matrix, MESH: Molecular Chaperones, Intermembrane space, Saccharomyces cerevisiae Proteins, MESH: Mitochondria, MESH: Biological Transport, SOD1, chemistry.chemical_element, MESH: Phenotype, Electron Transport Complex IV, Superoxide dismutase, 03 medical and health sciences, MESH: Electron Transport Complex IV, MESH: Glycerol, Humans, Cytochrome c oxidase, Inner membrane, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, 030304 developmental biology, MESH: Humans, Superoxide Dismutase, MESH: Cytoplasm, Genetic Complementation Test, MESH: Metallothionein, Biological Transport, Cell Biology, Copper, Oxidative Stress, chemistry, biology.protein, Metallothionein, 030217 neurology & neurosurgery, Molecular Chaperones
Abstract

International audience; A mitochondrial matrix copper ligand (CuL) complex, conserved in mammalian cells, is the likely source of copper for assembly of cytochrome c oxidase (CcO) and superoxide dismutase 1 (Sod1) within the intermembrane space (IMS) in yeast. Targeting the copper-binding proteins human Sod1 and Crs5 to the mitochondrial matrix results in growth impairment on non-fermentable medium caused by decreased levels of CcO. This effect is reversed by copper supplementation. Matrix-targeted Crs5 diminished Sod1 protein within the IMS and impaired activity of an inner membrane tethered human Sod1. Copper binding by the matrix-targeted proteins attenuates levels of the CuL complex without affecting total mitochondrial copper. These data suggest that attenuation of the matrix CuL complex via heterologous competitors limits available copper for metallation of CcO and Sod1 within the IMS. The ligand also exists in the cytoplasm in an apparent metal-free state.

Published
2006

22. The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding

Author

Yih-Chern Horng, Eric A. Shoubridge, Florin Sasarman, Dennis R. Winge, Fabien Pierrel, Scot C. Leary, Paul A. Cobine, University of Utah, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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), Department of Human Genetics [Montréal], and McGill University = Université McGill [Montréal, Canada]

Subjects
MESH: Mutation, Mitochondrial translation, MESH: Mitochondria, Protein subunit, Mutation, Missense, MESH: Carrier Proteins, Biology, medicine.disease_cause, Biochemistry, Electron Transport Complex IV, MESH: Recombinant Proteins, 03 medical and health sciences, Copper Transport Proteins, COX17, MESH: Electron Transport Complex IV, Mutant protein, medicine, Humans, Missense mutation, Cytochrome c oxidase, MESH: Protein Binding, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, 030304 developmental biology, 0303 health sciences, Mutation, MESH: Mutation, Missense, Binding Sites, MESH: Humans, 030302 biochemistry & molecular biology, Membrane Proteins, Translation (biology), Cell Biology, Fibroblasts, Molecular biology, Recombinant Proteins, Mitochondria, MESH: Copper, MESH: Binding Sites, MESH: Fibroblasts, biology.protein, MESH: Membrane Proteins, Carrier Proteins, Copper, Molecular Chaperones, Protein Binding
Abstract

International audience; Sco1 is a metallochaperone that is required for copper delivery to the Cu(A) site in the CoxII subunit of cytochrome c oxidase. The only known missense mutation in human Sco1, a P174L substitution in the copper-binding domain, is associated with a fatal neonatal hepatopathy; however, the molecular basis for dysfunction of the protein is unknown. Immortalized fibroblasts from a SCO1 patient show a severe deficiency in cytochrome c oxidase activity that was partially rescued by overexpression of P174L Sco1. The mutant protein retained the ability to bind Cu(I) and Cu(II) normally when expressed in bacteria, but Cox17-mediated copper transfer was severely compromised both in vitro and in a yeast cytoplasmic assay. The corresponding P153L substitution in yeast Sco1 was impaired in suppressing the phenotype of cells harboring the weakly functional C57Y allele of Cox17; however, it was functional in sco1delta yeast when the wild-type COX17 gene was present. Pulse-chase labeling of mitochondrial translation products in SCO1 patient fibroblasts showed no change in the rate of CoxII translation, but there was a specific and rapid turnover of CoxII protein in the chase. These data indicate that the P174L mutation attenuates a transient interaction with Cox17 that is necessary for copper transfer. They further suggest that defective Cox17-mediated copper metallation of Sco1, as well as the subsequent failure of Cu(A) site maturation, is the basis for the inefficient assembly of the cytochrome c oxidase complex in SCO1 patients.

Published
2006

23. Overexpression of cellular prion protein induces an antioxidant environment altering T cell development in the thymus

Author

Jacqueline Riondel, Jean-Yves Cesbron, Marianne M. A. Martinic, Valérie Attuil-Audenis, Catherine Aude-Garcia, Alain Favier, Carole Siret, Patrice N. Marche, Evelyne Jouvin-Marche, Christian L. Villiers, Christoph Huber, Philippe Naquet, Valérie Podevin-Dimster, Walid Rachidi, Mark D. Zabel, Contrôle moléculaire de la réponse immune specifique, Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF), Laboratoire de biologie du stress oxydant, Université Joseph Fourier - Grenoble 1 (UJF), Neuropathology institute, University hospital of Zurich [Zurich], Transmission et pathogénèse des maladies à prions (TPMP), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Institute of experimental immunology, grants from the Groupement d'Inte´reˆt Scientifique- Prion (Grants A42 and A108), the Commissariat a` l'Energie Atomique Tox- Nuc Program (Grant 13-10), and the European Union, Project Number QLK5-CT- 2002-01044. V.A.-A. is a recipient of a GIS-Prion Fellowship., Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), and Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Cellular differentiation, Receptors, Antigen, T-Cell, alpha-beta, T-Lymphocytes, MESH: Dietary Supplements, Antioxidants, Mice, 0302 clinical medicine, T lymphocyte, Immunology and Allergy, MESH: Animals, Receptor, MESH: Antigens, CD, Regulation of gene expression, 0303 health sciences, MESH: Receptors, Antigen, T-Cell, alpha-beta, Cell Differentiation, MESH: Gene Expression Regulation, Thymus, MESH: Copper, medicine.anatomical_structure, Phenotype, Prion, [SDV.IMM]Life Sciences [q-bio]/Immunology, MESH: Cell Differentiation, MESH: Mice, Transgenic, Prions, Transgene, T cell, Oxydative Stress, Immunology, Context (language use), Mice, Transgenic, Thymus Gland, Biology, MESH: Phenotype, 03 medical and health sciences, MESH: Prions, Antigen, MESH: Mice, Inbred C57BL, Antigens, CD, medicine, Animals, MESH: Mice, 030304 developmental biology, MESH: Antioxidants, MESH: Thymus Gland, Molecular biology, Mice, Inbred C57BL, MESH: T-Lymphocytes, Gene Expression Regulation, Dietary Supplements, 030217 neurology & neurosurgery, Copper
Abstract

E.J.-M, V.A.-A. and C.A.-G. contributed equally to this work.; International audience; Cellular prion protein (PrP(C)) is an ubiquitously expressed glycoprotein whose roles are still widely discussed, particularly in the field of immunology. Using TgA20- and Tg33-transgenic mice overexpressing PrP(C), we investigated the consequences of this overexpression on T cell development. In both models, overexpression of PrP(C) induces strong alterations at different steps of T cell maturation. On TgA20 mice, we observed that these alterations are cell autonomous and lead to a decrease of alphabeta T cells and a concomitant increase of gammadelta T cell numbers. PrP(C) has been shown to bind and chelate copper and, interestingly, under a copper supplementation diet, TgA20 mice presented a partial restoration of the alphabeta T cell development, suggesting that PrP(C) overexpression, by chelating copper, generates an antioxidant context differentially impacting on alphabeta and gammadelta T cell lineage.

Published
2006

24. HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions

Author

Daphné Seigneurin-Berny, Pierre Richaud, Giovanni Finazzi, Norbert Rolland, Antoine Gravot, Alexandra Kraut, Christophe Mazard, Pascaline Auroy, Jacques Joyard, Didier Grunwald, Fabrice Rappaport, Alain Vavasseur, Roux-Buisson, Nathalie, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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), Laboratoire des Echanges Membranaires et Signalisation (LEMS), Université de la Méditerranée - Aix-Marseille 2-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Physiologie membranaire et moléculaire du chloroplaste (PMMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), ANTE-INSERM U836, équipe 4, Muscles et pathologies, Laboratoire Canaux Ioniques, Fonctions et Pathologies, EMI 9931 CEA/INSERM/Universite' Joseph Fourier-DRDC/ CEA-Grenoble-EMI 9931 CEA/INSERM/Universite' Joseph Fourier-DRDC/ CEA-Grenoble, This work was supported by CNRS and CEA (Toxicologie Nucléaire Environnementale) research programs., Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)

Subjects
0106 biological sciences, enveloppe chloroplastique, Chloroplasts, Light, ATPase, Mutant, Arabidopsis, MESH: Amino Acid Sequence, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], 01 natural sciences, Biochemistry, Chloroplast membrane, protéine transmembranaire, Yeasts, Homeostasis, MESH: Arabidopsis, Cloning, Molecular, Plastocyanin, Cation Transport Proteins, MESH: Superoxide Dismutase, Plant Proteins, Adenosine Triphosphatases, 0303 health sciences, chloroplaste, biology, MESH: Plant Proteins, ion métallique, MESH: Yeasts, zinc, stress lumineux, food and beverages, Chloroplast, MESH: Copper, cuivre, Chloroplast DNA, plante expérimentale, MESH: Homeostasis, Copper-transporting ATPases, MESH: Mutation, Nuclear Envelope, Molecular Sequence Data, MESH: Arabidopsis Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, TRANSPORT INTRACELLULLAIRE, 03 medical and health sciences, MESH: Nuclear Envelope, MESH: Cation Transport Proteins, [SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], MESH: Adenosine Triphosphatases, MESH: Cloning, Molecular, Amino Acid Sequence, Molecular Biology, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, homéostasie, 030304 developmental biology, Ion Transport, MESH: Molecular Sequence Data, MESH: Chloroplasts, Arabidopsis Proteins, Superoxide Dismutase, arabidopsis thaliana, Cell Biology, biology.organism_classification, MESH: Light, MESH: Ion Transport, Copper-Transporting ATPases, Mutation, biology.protein, Copper, 010606 plant biology & botany
Abstract

International audience; Although ions play important roles in the cell and chloroplast metabolism, little is known about ion transport across the chloroplast envelope. Using a proteomic approach specifically targeted to the Arabidopsis chloroplast envelope, we have identified HMA1, which belongs to the metal-transporting P1B-type ATPases family. HMA1 is mainly expressed in green tissues, and we validated its chloroplast envelope localization. Yeast expression experiments demonstrated that HMA1 is involved in copper homeostasis and that deletion of its N-terminal His-domain partially affects the metal transport. Characterization of hma1 Arabidopsis mutants revealed a lower chloroplast copper content and a diminution of the total chloroplast superoxide dismutase activity. No effect was observed on the plastocyanin content in these lines. The hma1 insertional mutants grew like WT plants in standard condition but presented a photosensitivity phenotype under high light. Finally, direct biochemical ATPase assays performed on purified chloroplast envelope membranes showed that the ATPase activity of HMA1 is specifically stimulated by copper. Our results demonstrate that HMA1 offers an additional way to the previously characterized chloroplast envelope Cu-ATPase PAA1 to import copper in the chloroplast.

Published
2006

25. A field method using microcosms to evaluate transfer of Cd, Cu, Ni, Pb and Zn from sewage sludge amended forest soils to Helix aspersa snails

Author

A. Gomot-de Vaufleury, Pierre-Marie Badot, Jean-Michel Carnus, M Ben Brahim, Renaud Scheifler, Laboratoire Chrono-environnement ( LCE ), Université Bourgogne Franche-Comté ( UBFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Franche-Comté ( UFC ), Centre de Sfax, Institut National de la Recherche Agronomique ( INRA ), Laboratoire Chrono-environnement - UFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Institut National de la Recherche Agronomique (INRA), Laboratoire Chrono-environnement - CNRS - UBFC (UMR 6249) (LCE), Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), and Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)

Subjects
MESH : Biological Availability, Health, Toxicology and Mutagenesis, MESH: Forestry, [ SDV.TOX.ECO ] Life Sciences [q-bio]/Toxicology/Ecotoxicology, 010501 environmental sciences, Toxicology, 01 natural sciences, MESH: Zinc, MESH : Soil Pollutants, Food chain, Nickel, MESH: Helix (Snails), Biomonitoring, MESH: Nickel, Soil Pollutants, MESH: Animals, MESH : Environmental Monitoring, MESH : Copper, MESH : Cadmium, MESH: Biological Availability, Sewage, biology, Chemistry, Helix (gastropod), Forestry, 04 agricultural and veterinary sciences, General Medicine, Pollution, 6. Clean water, MESH: Copper, Zinc, Metals, Environmental chemistry, MESH : Helix (Snails), [SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/Ecotoxicology, MESH : Lead, Microcosm, MESH: Environmental Monitoring, MESH: Lead, Cadmium, Environmental Monitoring, MESH: Cadmium, Biological Availability, Animals, MESH: Sewage, 0105 earth and related environmental sciences, Invertebrate, MESH: Soil Pollutants, MESH: Metals, Helix, Snails, MESH : Metals, MESH : Zinc, biology.organism_classification, Bioavailability, Lead, MESH : Sewage, Soil water, 040103 agronomy & agriculture, MESH : Forestry, 0401 agriculture, forestry, and fisheries, MESH : Animals, MESH : Nickel, Copper, Sludge
Abstract

International audience; Juvenile Helix aspersa snails exposed in field microcosms were used to assess the transfer of Cd, Cu, Ni, Pb and Zn from forest soils amended with liquid and composted sewage sludge. Zn concentrations and contents were significantly higher in snails exposed to liquid and composted sludge after 5 and 7 weeks of exposure, when compared with control. Trends were less clear for the other metals. Present results show that Zn, among the cocktail of metallic trace elements (MTE) coming from sewage sludge disposal, represents the principal concern for food chain transfer and secondary poisoning risks. The microcosm design used in this experiment was well suited for relatively long-term (about 2 months) active biomonitoring with H. aspersa snails. The snails quickly indicated the variations of MTE concentrations in their immediate environment. Therefore, the present study provides a simple but efficient field tool to evaluate MTE bioavailability and transfer.

Published
2002

26. The Pleiotropic CymR Regulator of Staphylococcus aureus Plays an Important Role in Virulence and Stress Response

Author

Sarah Dubrac, Tarek Msadek, Olivier Poupel, Isabelle Martin-Verstraete, Olga Soutourina, Génétique des Génomes Bactériens, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Biologie des Bactéries Pathogènes à Gram-positif, I. M-V. and O. S. are full and assistant professors at the Université Paris 7, respectively. Research was supported by grants from the Centre National de la Recherche Scientifique (CNRS URA 2171 and 2172), the Institut Pasteur (Grand Programme Horizontal N°9 and PTR N°256) and the European Commission for the group of T. M. (Grants StaphDynamics, LHSM-CT-2006-019064, and BaSysBio, LSHG-CT-2006-037469)., We are grateful to S. Foster for providing us with S. aureus strains and valuable discussions. We thank O. Sismeiro, C. Lacroix and J.-Y. Coppee for macroarray preparation, S. Rousseau and P. Vantadour for loading transcriptome data onto the Genoscript database and P. Courtin for metabolite analysis., European Project: 35105,STAPHDYNAMICS, European Project: 38901,BASYSBIO, and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV]Life Sciences [q-bio], Mutant, MESH: Virulence, medicine.disease_cause, Mice, chemistry.chemical_compound, MESH: Oxidants, MESH: Staphylococcus aureus, MESH: Up-Regulation, Homeostasis, MESH: Animals, Disulfides, lcsh:QH301-705.5, Pathogen, Regulation of gene expression, Mice, Inbred BALB C, 0303 health sciences, MESH: Oxidative Stress, Virulence, Staphylococcal Infections, Oxidants, Up-Regulation, MESH: Copper, MESH: Tellurium, MESH: Homeostasis, Staphylococcus aureus, Cystine, MESH: Hydrogen Peroxide, Microbiology/Microbial Physiology and Metabolism, Female, Tellurium, MESH: Genes, Bacterial, Microbiology/Cellular Microbiology and Pathogenesis, Intracellular, Research Article, lcsh:Immunologic diseases. Allergy, Immunology, MESH: Mice, Inbred BALB C, MESH: Staphylococcal Infections, Biology, Microbiology, Cell Line, 03 medical and health sciences, Virology, Genetics, medicine, Animals, MESH: Disulfides, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Mice, Molecular Biology, Cysteine metabolism, 030304 developmental biology, Metal ion homeostasis, 030306 microbiology, Macrophages, MESH: Macrophages, MESH: Cystine, Hydrogen Peroxide, MESH: Cell Line, Oxidative Stress, lcsh:Biology (General), chemistry, Genes, Bacterial, MESH: Gene Deletion, Parasitology, lcsh:RC581-607, MESH: Female, Copper, Gene Deletion
Abstract

We have characterized a novel pleiotropic role for CymR, the master regulator of cysteine metabolism. We show here that CymR plays an important role both in stress response and virulence of Staphylococcus aureus. Genes involved in detoxification processes, including oxidative stress response and metal ion homeostasis, were differentially expressed in a ΔcymR mutant. Deletion of cymR resulted in increased sensitivity to hydrogen peroxide-, disulfide-, tellurite- and copper-induced stresses. Estimation of metabolite pools suggests that this heightened sensitivity could be the result of profound metabolic changes in the ΔcymR mutant, with an increase in the intracellular cysteine pool and hydrogen sulfide formation. Since resistance to oxidative stress within the host organism is important for pathogen survival, we investigated the role of CymR during the infectious process. Our results indicate that the deletion of cymR promotes survival of S. aureus inside macrophages, whereas virulence of the ΔcymR mutant is highly impaired in mice. These data indicate that CymR plays a major role in virulence and adaptation of S. aureus for survival within the host., Author Summary Staphylococcus aureus is a very harmful human pathogen that is a major cause of nosocomial infections. Humans have developed sophisticated defense strategies against invading bacteria, including the innate immune response, with the generation of an oxidative burst inside phagocytic cells. Staphylococcal infections are extremely difficult to eradicate due to the remarkable capacity of these bacteria to adapt to different environmental conditions both inside and outside the host organism. Sulfur metabolism is essential for all living organisms and is tightly controlled by regulatory proteins. In this paper, we revealed an important role for CymR, a major regulator of sulfur metabolism, in adaptation of S. aureus to the host environment. Inactivation of the gene encoding this regulator in S. aureus leads to a mutant bacterium with increased vulnerability to stress conditions including oxidative stress encountered inside the host. More importantly, the deletion of the cymR gene strongly affected the interaction of S. aureus with its host, leading to impaired virulence in mice. Our results place CymR among the potential targets for attenuation of S. aureus infections.

Published
2010

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