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Bacillus anthracis Spores Influence ATP Synthase Activity in Murine Macrophages  

Seo, Gwi-Moon (Division of Molecular and Life Sciences, Hanyang University)
Jung, Kyoung-Hwa (Division of Molecular and Life Sciences, Hanyang University)
Kim, Seong-Joo (Division of Molecular and Life Sciences, Hanyang University)
Kim, Ji-Cheon (Division of Molecular and Life Sciences, Hanyang University)
Yoon, Jang-Won (Division of Molecular and Life Sciences, Hanyang University)
Oh, Kwang-Keun (Department of Bioprocess Technology, BioPolytechnic College)
Lee, Jung-Ho (Department of Chemical Engineering, Hanyang University)
Chai, Young-Gyu (Division of Molecular and Life Sciences, Hanyang University)
Publication Information
Journal of Microbiology and Biotechnology / v.18, no.4, 2008 , pp. 778-783 More about this Journal
Abstract
Anthrax is an infectious disease caused by toxigenic strains of the Gram-positive bacterium Bacillus anthracis. To identify the mitochondrial proteins that are expressed differently in murine macrophages infected with spores of B. anthracis Sterne, proteomic and MALDI-TOF/MS analyses of uninfected and infected macrophages were conducted. As a result, 13 mitochondrial proteins with different expression patterns were discovered in the infected murine macrophages, and some were identified as ATP5b, NIAP-5, ras-related GTP binding protein B isoform CRAa, along with several unnamed proteins. Among these proteins, ATP5b is related to energy production and cytoskeletal rearrangement, whereas NIAP-5 causes apoptosis of host cells due to binding with caspase-9. Therefore, this paper focused on ATP5b, which was found to be down regulated following infection. The downregulated ATP5b also reduced ATP production in the murine macrophages infected with B. anthracis spores. Consequently, this study represents the first mitochondrial proteome analysis of infected macrophages.
Keywords
Bacillus anthracis spores; mass spectrometry; mitochondrial proteomics; murine macrophages;
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Times Cited By Web Of Science : 3  (Related Records In Web of Science)
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1 Galmiche, A., J. Rassow, A. Doye, S. Cagnol, J. C. Chambard, S. Contamin, V. de Thillot, I. Just, V. Ricci, E. Solcia, E. Van Obberqhen, and P. Boquet. 2000. The N-terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release. EMBO J. 19: 6361-6370   DOI   ScienceOn
2 Joiner, K. A. 1997. Membrane-protein traffic in pathogeninfected cells. J. Clin. Invest. 99: 1814-1817   DOI   ScienceOn
3 Oakley, B. R., D. R. Kirsch, and N. R. Morris. 1980. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105: 361-363   DOI   ScienceOn
4 Seo, G. M., S. J. Kim, and Y. G. Chai. 2004. Rapid profiling of the infection of Bacillus anthracis on human macrophages using SELDI-TOF mass spectroscopy. Biochem. Biophys. Res. Commun. 325: 1236-1239   DOI   ScienceOn
5 Willhite, D. C. and S. R. Blanke. 2004. Helicobacter pylori vacuolating cytotoxin enters cells, localizes to the mitochondria, and induces mitochondrial membrane permeability changes correlated to toxin channel activity. Cell. Microbiol. 6: 143- 154   DOI   ScienceOn
6 Willhite, D. C., T. L. Cover, and S. R. Blanke. 2003. Cellular vacuolation and mitochondrial cytochrome c release are independent outcomes of Helicobacter pylori vacuolating cytotoxin activity that are each dependent on membrane channel formation. J. Biol. Chem. 278: 48204-48209   DOI   ScienceOn
7 Tonge, R., J. Shaw, B. Middleton, R. Rowlinson, S. Rayner, and J. Young. 2001. Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 1: 377-396   DOI   ScienceOn
8 Park, T. J., J. P. Park, G. M. Seo, Y. G. Chai, and S. Y. Lee. 2006. Rapid and accurate detection of Bacillus anthracis spores using peptide-quantum dot conjugates. J. Microbiol. Biotechnol. 16: 1713-1719   과학기술학회마을
9 Chandra, H., P. K. Gupta, K. Sharma, A. R. Mattoo, S. K. Garg, W. N. Gade, R. Sirdeshmukh, K. Maithal, and Y. Singh. 2005. Proteome analysis of mouse macrophages treated with anthrax lethal toxin. Biochim. Biophys. Acta 1747: 151-159   DOI   ScienceOn
10 Guidi-Rontani, C., M. Weber-Levy, E. Labruyere, and M. Mock. 1999. Germination of Bacillus anthracis spores within alveolar macrophages. Mol. Microbiol. 31: 9-17   DOI   ScienceOn
11 Kim, H. T., G. W. Seo, K. Y. Jung, S. J. Kim, J. C. Kim, K. G. Oh, B. S. Koo, and Y. G. Chai. 2007. Generation of a specific marker to discriminate Bacillus anthracis from other bacteria of the Bacillus cereus group. J. Microbiol. Biotechnol. 17: 806- 811   과학기술학회마을
12 Kovarova, H., P. Halada, P. Man, I. Golovliov, Z. Krocova, J. Spacek, S. Porkertova, and R. Necasova. 2002. Proteome study of Francisella tularensis live vaccine strain-containing phagosome in Bcg/Nramp1 congenic macrophages: Resistant allele contributes to permissive environment and susceptibility to infection. Proteomics 2: 85-93   DOI   ScienceOn
13 Samali, A., J. Cai, B. Zhivotovsky, D. P. Jones, and S. Orrenius. 1999. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells. EMBO J. 18: 2040-2048   DOI   ScienceOn
14 Dixon, T. C., A. A. Fadl, T. M. Koehler, J. A. Swanson, and P. C. Hanna. 2000. Early Bacillus anthracis-macrophage interactions: Intracellular survival and escape. Cell. Microbiol. 2: 453-463   DOI   ScienceOn
15 Guidi-Rontani, C. 2002. The alveolar macrophage: The Trojan horse of Bacillus anthracis. Trends Microbiol. 10: 405-409   DOI   ScienceOn
16 Polla, B. S., D. Francois, S. Salvioli, G. Franceschi, C. Marsac, and A. Cossarizza. 1996. Mitochondria are selective targets for the protective effects of heat shock against oxidative injury. Proc. Natl. Acad. Sci. USA 93: 6458-6463
17 Stephen, J. 1981. Anthrax toxin. Pharmacol. Therap. 12: 501- 513   DOI   ScienceOn
18 Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254   DOI   ScienceOn
19 Yamasaki, E., A. Wada, A. Kumatori, I. Nakagawa, J. Funao, M. Nakayama, J. Hisatsune, M. Kimura, J. Moss, and T. Hirayama. 2006. Helicobacter pylori vacuolating cytotoxin induces activation of the proapoptotic proteins Bax and Bak, leading to cytochrome c release and cell death, independent of vacuolation. J. Biol. Chem. 281: 11250-11259   DOI   ScienceOn
20 Kim, I. S., H. S. Yun, and I. N. Jin. 2007. Comparative proteomic analyses of the yeast Saccharomyces cerevisiae KNU5377 strain again menadion-induced oxidative stress. J. Microbiol. Biotechnol. 17: 207-217   과학기술학회마을
21 Seo, G. M., S. J. Kim, J. C. Kim, D. H. Nam, M. Y. Yoon, B. S. Koo, and Y. G. Chai. 2004. Targeting of Bacillus anthracis interaction factors for human macrophages using two-dimensional gel electrophoresis. Biochem. Biophys. Res. Commun. 322: 854-859   DOI   ScienceOn
22 Sapra, R., S. P. Gaucher, J. S. Lachmann, G. M. Buffleben, G. S. Chirica, J. E. Comer, J. W. Peterson, A. K. Chopra, and A. K. Singh. 2006. Proteomic analyses of murine macrophages treated with Bacillus anthracis lethal toxin. Microb. Pathogen. 41: 157-167   DOI   ScienceOn
23 Kuhn, J. F., P. Hoerth, S. T. Hoehn, T. Preckel, and K. B. Tomer. 2006. Proteomics study of anthrax lethal toxin-treated murine macrophages. Electrophoresis 27: 1584-1597   DOI   ScienceOn
24 Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858   DOI   ScienceOn