Abstract:Reactive oxygen (nitrogen) species are intermediates of body’s metabolism, active and strong oxidizing property. The microenvironment of activated macrophages have a mass of reactive oxygen and nitrogen species to inhibit or kill the alien pathogens by destroying biofilms, changing the function of proteins and inducing gene mutation. Mycobacterium tuberculosis can not only survive in macrophage, but also increase to large numbers. Oxidative or nitrosative stress will result in massive transcriptional changes which can help Mycobacterium tuberculosis escape from the damage of reactive oxygen and nitrogen species. In this paper, we reviewed the recent research progress of Mycobacterium tuberculosis genes resisting to oxidative or nitrosative stress, and summarize the relationship of them.
付鑫, 王爱妍, 丁峰山, 何时义, 杨东君, 凌敏. 结核分枝杆菌耐受活性氧和活性氮基因的研究进展[J]. 中国人兽共患病学报, 2015, 31(9): 854-858.
FU Xin, WANG Ai-yan, DING Feng-shan, HE Shi-yi, YANG Dong-jun, LING Min. Research progress of Mycobacterium tuberculosis genes resisting to reactive oxygen and nitrogen species. Chinese Journal of Zoonoses, 2015, 31(9): 854-858.
[1] Mayer-Barber KD, Andrade BB, Oland SD, et al.Host-directed therapy of tuberculosis based on interleukin-1 and type I interferon crosstalk[J]. Nature, 2014 Jul 3, 511(7507): 99-103. doi:10.1038/nature13489. [2] World Health Organization. Global tuberculosis report 2013[R]. Globocan:World Health Organization 2013. [3] Pacheco SA, Hsu FF, Powers KM, et al. MmpL11 protein transports mycolic acid-containing lipids to the mycobacterial cell wall and contributes to biofilm formation in Mycobacterium smegmatis[J]. J Biological Chem, 2013, 288(33): 24213-24222.doi:10.1074/jbc.M113.473371. [4] Tripathi D, Chandra H, Bhatnagar R. Poly-L-glutamate/glutamine synthesis in the cell wall of Mycobacterium bovis is regulated in response to nitrogen availability[J]. BMC Microbiol, 2013, 13: 226. doi:10.1186/1471-2180-13-226. [5] Geier H, Mostowy S, Cangelosi GA, et al. Autoinducer-2 triggers the oxidative stress response in Mycobacterium avium , leading to biofilm formation[J]. Apply Environmental Microbiol, 2008, 74(6): 1798-1804. doi:10.1128/AEM.02066-07. [6] Sherman DR, Sabo PJ, Hickey MJ, et al. Disparate responses to oxidative stress in saprophytic and pathogenic mycobacteria[J]. Proceed Nat Acad Sci U S A, 1995, 92(14): 6625-6629. [7] Romay Z, Arraiz N, Fuenmayor A, et al. Detection of S315T mutation in the katg gene as a strategy for identification of isoniazid-resistant Mycobacterium tuberculosis in a reference laboratory[J]. Revista chilena de infectologia: órgoan oficial de la Sociedad Chilena de Infectologia, 2012, 29(6): 607-613. doi:10.4067/S0716-10182012000700004 [8] Ng VH, Cox JS, Sousa AO, et al. Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst[J]. Mol Microbiol, 2004, 52(5): 1291-1302. [9] Bryk R, Griffin P, Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins[J]. Nature, 2000, 407(6801): 211-215. [10] Njuma OJ, Ndontsa EN, Goodwin DC. Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG[J]. Arch Biochem Biophysics, 2014, 544: 27-39. doi:10.1016/j.abb.2013.11.007. [11] Vidossich P, Loewen PC, Carpena X, et al. Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation[J]. J Phys Chem B, 2014, 118(11): 2924-2931. doi:10.1021/jp4123425. [12] Olson AL, Neumann TS, Cai S, et al. Solution structures of Mycobacterium tuberculosis thioredoxin C and models of the intact thioredoxin system suggest new approaches to inhibitor and drug design[J]. Proteins, 2013, 81(4): 675-689. doi:10.1002/prot.24228. [13] Akif M, Khare G, Tyagi AK, et al. Functional studies of multiple thioredoxins from Mycobacterium tuberculosis [J]. J Bacteriol, 2008, 190(21): 7087-7095. doi:10.1128/JB.00159-08. [14] Tiwari D, Singh RK, Goswami K, et al. Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host[J]. J Biological Chem, 2009, 284(40): 27467-27479. doi:10.1074/jbc.M109.036095. [15] Akif M, Suhre K, Verma C, et al. Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis[J]. Acta Crystallographica. Sect D, Biological Crystallography, 2005, 61(Pt12): 1603-1611. [16] Guimaraes BG, Souchon H, Honore N, et al. Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress[J]. J Biological Chem, 2005, 280(27): 25735-25742. [17] Jaeger T, Budde H, Flohe L, et al. Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis [J]. Arch Biochem Biophys, 2004, 423(1): 182-191. [18] St John G, Brot N, Ruan J, et al. Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates[J]. Proceed Nat Acade Sci U S A, 2001, 98(17): 9901-9906. [19] Dhandayuthapani S, Jagannath C, Nino C, et al. Methionine sulfoxide reductase B (MsrB) of Mycobacterium smegmatis plays a limited role in resisting oxidative stress[J]. Tuberculosis (Edinb), 2009, 89 (Suppl)1: S26-32. doi:10.1016/S1472-9792(09)70008-3. [20] Taylor AB, Benglis DM Jr, Dhandayuthapani S, et al. Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine[J].J Bacteriol, 2003, 185: 8. [21] Douglas T, Daniel DS, Parida BK, et al. Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages[J]. J Bacteriol, 2004, 186(11): 3590-3598. [22] Gordon BR, Li Y, Wang L, et al. Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosi [J]. Proc Natl Acad Sci U S A, 2010, 107(11): 5154-5159. doi:10.1073/pnas.0913551107. [23] Colangeli R, Haq A, Arcus VL, et al. The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates[J]. Proc Natl Acad Sci U S A, 2009, 106(11): 4414-4418 doi:10.1073/pnas.0810126106. [24] Du Y, Zhang H, He Y, et al. Mycobacterium smegmatis Lsr2 physically and functionally interacts with a new flavoprotein involved in bacterial resistance to oxidative stress[J].J Biochem, 2012, 152(5): 479-486. doi:10.1093/jb/mvs095. [25] Park KT, Dahl JL, Bannantine JP, et al. Demonstration of allelic exchange in the slow-growing bacterium Mycobacterium avium subsp. paratuberculosis, and generation of mutants with deletions at the pknG, relA, and lsr2 loci[J]. Appl Environ Microbiol, 2008, 74(6):1687-1695. doi:10.1128/AEM.01208-07. [26] Bartek IL, Woolhiser LK, Baughn AD, et al. Mycobacterium tuberculosis Lsr2 is a global transcriptional regulator required for adaptation to changing oxygen levels and virulence[J]. MBio, 2014, 5(3): e01106-01114. doi:10.1128/mBio.01106-14. [27] Wu LT. Cloning and functional characterization of Mycobacterium tuberculosis NrdH-redoxin[D]. Chongqing Southwest university master's degree thesis, 2010. 吴雷婷. 结核分枝杆菌NrdH-redoxin基因的克隆、表达及功能研究[D]. 重庆: 西南大学, 2010. [28] Si MR, Zhang L, Yang ZF, et al. NrdH redoxin enhances resistance to multiple oxidative stresses by acting as a peroxidase cofactor in Corynebacterium glutamicum[J]. Appl Environmental Microbiol, 2014, 80(5): 1750-1762. doi:10.1128/AEM.03654-13. [29] Van Laer K, Dziewulska AM, Fislage M, et al. NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase[J]. J B Chem, 2013, 288(11): 7942-7955. doi:10.1074/jbc.M112.392688. [30] Ehrt BS,Shiloh MU,Ruan J, et al. A novel antioxidant gene from Mycobacterium tuberculosis [J]. J Expel Med, 1997, 186(11): 1885-1896. [31] Ruan J, St John G, Ehrt S, et al. noxR3, a novel gene from Mycobacterium tuberculosis , protects Salmonella typhimurium from nitrosative and oxidative stress[J]. Infect Immun, 1999, 67(7): 3276-3283. [32] Stewart GR, Ehrt S, Riley LW, et al. Deletion of the putative antioxidant noxR1 does not alter the virulence of Mycobacterium tuberculosis H37Rv[J]. Tubercle Lung Dis :Official J Int Union Aainst Tuberculosis Lung Dis, 2000, 80(4-5): 237-242.