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1. Mycobacterial P1-Type ATPases Mediate Resistance to Zinc Poisoning in Human Macrophages

Author

Paola Ricciardi Castagnoli, Simon J. Waddell, Isabelle Maridonneau-Parini, Pascale Peyron, Sylvain Tilleul, Renaud Poincloux, Ludovic Tailleux, Yannick Poquet, Chantal de Chastellier, Qian Gao, Philip D. Butcher, Florence Levillain, Chuan Wang, Hélène Botella, Olivier Neyrolles, Guillaume M. Charrière, Brigitte Gicquel, Geanncarlo Lugo-Villarino, Irène Brandli, Maria Foti, Institut de pharmacologie et de biologie structurale (IPBS), Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Dynamique de la membrane et du cytosquelette, Compartimentation et dynamique cellulaires (CDC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Department of Medical Sciences, Key Laboratory of Medical Molecular Virology - Fudan University, Fudan University [Shanghai], Génétique mycobactérienne - Mycobacterial genetics, Institut Pasteur [Paris] (IP), Neurobiologie, plasticité tissulaire et métabolisme énergétique (NPTME), Brighton and Sussex Medical School (BSMS), Università degli Studi di Milano-Bicocca = University of Milano-Bicocca (UNIMIB), St George's, University of London, Singapore Immunology Network (SIgN), Biomedical Sciences Institute (BMSI), Génétique et biochimie des microorganismes (GBM), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Institut Pasteur [Paris], Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano-Bicocca [Milano] (UNIMIB), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Botella, H, Levillain, F, Poincloux, R, Poquet, Y, Brandli, I, Wang, C, Tailleux, L, Tilleul, S, Charriere, G, Waddel, S, Foti, M, Lugo Villarino, G, Gao, Q, Maridonneau Parini, I, Castagnoli, P, De Chastellier, C, and Neyrolles, O

Subjects
Cancer Research, MESH: Mycobacterium tuberculosis, ATPase, medicine.disease_cause, Q1, MESH: Zinc, Mice, Mycobacterium Tuberculosis, macrophages, Metal poisoning, MESH: Animals, MESH: Tuberculosis, Cells, Cultured, Phagosome, 0303 health sciences, Mice, Inbred BALB C, MED/04 - PATOLOGIA GENERALE, 3. Good health, Zinc, QR180, [SDV.IMM]Life Sciences [q-bio]/Immunology, Female, Efflux, Intracellular, MESH: Cells, Cultured, MESH: Mice, Inbred BALB C, chemistry.chemical_element, Biology, Microbiology, Article, 03 medical and health sciences, Virology, Immunology and Microbiology(all), MESH: Bacterial Proton-Translocating ATPases, medicine, Animals, Humans, Tuberculosis, MESH: Mice, Molecular Biology, 030304 developmental biology, QR0075, MESH: Humans, 030306 microbiology, Macrophages, MESH: Macrophages, Mycobacterium tuberculosis, chemistry, Cytoplasm, Bacterial Proton-Translocating ATPases, Zinc toxicity, biology.protein, Parasitology, MESH: Female
Abstract

Summary Mycobacterium tuberculosis thrives within macrophages by residing in phagosomes and preventing them from maturing and fusing with lysosomes. A parallel transcriptional survey of intracellular mycobacteria and their host macrophages revealed signatures of heavy metal poisoning. In particular, mycobacterial genes encoding heavy metal efflux P-type ATPases CtpC, CtpG, and CtpV, and host cell metallothioneins and zinc exporter ZnT1, were induced during infection. Consistent with this pattern of gene modulation, we observed a burst of free zinc inside macrophages, and intraphagosomal zinc accumulation within a few hours postinfection. Zinc exposure led to rapid CtpC induction, and ctpC deficiency caused zinc retention within the mycobacterial cytoplasm, leading to impaired intracellular growth of the bacilli. Thus, the use of P1-type ATPases represents a M. tuberculosis strategy to neutralize the toxic effects of zinc in macrophages. We propose that heavy metal toxicity and its counteraction might represent yet another chapter in the host-microbe arms race., Highlights ► Zinc accumulates in the M. tuberculosis (Mtb) phagosome in macrophages (Mϕ) ► Mtb P1-type ATPases, including CtpC, are induced upon exposure to zinc inside Mϕ ► CtpC enables Mtb resistance to zinc poisoning and intracellular survival in Mϕ ► P1-type zinc efflux ATPase ZntA null E. coli is highly susceptible to Mϕ killing

Published
2011
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2. Electron competition process in respiratory chain: Regulatory mechanisms and physiological functions

Author

Arnaud Mourier, Louis Casteilla, Michel Rigoulet, Anne Galinier, Anne Devin, Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Neurobiologie, plasticité tissulaire et métabolisme énergétique (NPTME), Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)

Subjects
Saccharomyces cerevisiae Proteins, media_common.quotation_subject, Genes, Fungal, Saccharomyces cerevisiae, Respiratory chain, Biophysics, Oxidative phosphorylation, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Mitochondrion, Redox, Biochemistry, Competition (biology), Electron Transport, Oxygen Consumption, Dehydrogenases, ComputingMilieux_MISCELLANEOUS, media_common, Electron competition, Proton leak, biology, Respiratory chain supramolecular organization, Quinones, NADH dehydrogenase, Proton-Motive Force, NADH Dehydrogenase, Cell Biology, biology.organism_classification, Yeast, Quinone, Mitochondria, Mutation, biology.protein, Oxidation-Reduction
Abstract

In mitochondria isolated from the yeast Saccharomyces cerevisiae, under non-phosphorylating conditions, we have previously shown that there is a right of way for electrons coming from the external NADH dehydrogenase, Nde1p. In this work, we show that the electron competition process is identical under more physiological conditions i.e. oxidative phosphorylation. Such a competition generates a priority for cytosolic NADH reoxidation. Furthermore, this electron competition process is associated with an energy wastage (the “active leak”) that allows an increase in redox equivalent oxidation when the redox pressure increases. When this redox pressure is decreased, i.e. under phosphorylating conditions, most of this energy wastage is alleviated. By studying mutant strains affected either in respiratory chain supramolecular organization or in electron competition activity, we show that the respiratory chain supramolecular organization is not responsible for the electron competition processes. Moreover, we show two distinct relationships between the respiratory rate and the quinone redox state that seem to indicate two quinone pools that are involved in the electron right of way. Indeed, the more reduced pool would be associated to the electron right of way for the external dehydrogenases whereas the less reduced pool would be associated to the electron right of way for the internal dehydrogenases.

Published
2010

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