1887

Abstract

In (renamed ) glucose 6-phosphate (G6P) level is exceptionally high as compared to other bacteria, for example. Earlier investigations have indicated that G6P protects (Msm) against oxidative stress-inducing agents. G6P is a glycolytic intermediate formed either directly through the phosphorylation of glucose or indirectly via the gluconeogenic pathway. Its consumption is catalysed by several enzymes, one of which being the NADPH dependent G6P dehydrogenase (G6PDH) encoded by ). While investigating the extent to which the carbon sources glucose and glycerol influence Msm growth, we observed that intracellular concentration of G6P was lower in the former’s presence than the latter. We could correlate this difference with that in the growth rate, which was higher in glycerol than glucose. We also found that lowering of G6P content in glucose-grown cells was triggered by the induced expression of and the resultant increase in G6PDH activity. When we silenced using CRISPR-Cas9 technology, we observed a significant rise in the growth rate of Msm. Therefore, we have found that depletion of G6P in glucose-grown cells due to increased G6PDH activity is at least one reason why the growth rate of Msm in glucose is less than glycerol. However, we could not establish a similar link-up between slow growth in glucose and lowering of G6P level in the case of (Mtb). Mycobacteria, therefore, may have evolved diverse mechanisms to ensure that they use glycerol preferentially over glucose for their growth.

Funding
This study was supported by the:
  • Council of Scientific and Industrial Research
    • Principle Award Recipient: AnikBarman
  • Bose Institute, Kolkata
    • Principle Award Recipient: PoulamiGhosh
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2021-07-08
2024-11-03
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References

  1. Tiberi S, Migliori GB, Muhwa Chakaya J, Kaesava T, Al Abri SS et al. Commemorating World TB Day 2020: “IT’S TIME” - It’s time to End the Global TB Epidemic. Int J Infect Dis 2020; 92S:S1–S4 [View Article] [PubMed]
    [Google Scholar]
  2. Queval CJ, Brosch R, Simeone R. The macrophage: A disputed fortress in the battle against Mycobacterium tuberculosis. Front Microbiol 2017; 8:2284 [View Article] [PubMed]
    [Google Scholar]
  3. Cambau E, Drancourt M. Steps towards the discovery of Mycobacterium tuberculosis by Robert Koch, 1882. Clin Microbiol Infect 2014; 20:196–201 [View Article] [PubMed]
    [Google Scholar]
  4. Nocard ME, Roux E. On the bacilli culture of tuberculosis. Ann Inst Pasteur 1887; 1:19–29
    [Google Scholar]
  5. Loebel RO, Shorr E, Richardson HB. The influence of foodstuffs upon the respiratory metabolism and growth of human tubercle bacilli. J Bacteriol 1933; 26:139–166
    [Google Scholar]
  6. Nakamura T. Uber die atmung der Tuberkelbazillen. Tohoku J Exp Med 1938; 34:
    [Google Scholar]
  7. Hunter GJE. The oxidation of glycerol by mycobacteria. J Biochem 1953; 55:320–328 [View Article]
    [Google Scholar]
  8. Wong SC. The relation between the growth of Mycobacterium tuberculosis and the yield of tuberculin on synthetic media. J Bacteriol 1937; 33:451–460 [View Article] [PubMed]
    [Google Scholar]
  9. Youmans GP, Youmans AS. Studies on the metabolism of Mycobacterium tuberculosis. I. The effect of carbohydrates and alcohols on the growth of Mycobacterium tuberculosis var. hominis. J Bacteriol 1953; 65:92–95 [View Article]
    [Google Scholar]
  10. de Carvalho LPS, Fischer SM, Marrero J, Nathan C, Ehrt S et al. Metabolomics of Mycobacterium tuberculosis reveals compartmentalized co-catabolism of carbon substrates. Chemistry & Biology 2010; 17:1122–1131 [View Article]
    [Google Scholar]
  11. Michelle M, Huang CC, Moss CE, Koh EI, Megan K. Common variants in the glycerol kinase gene reduce tuberculosis drug efficacy. mBio 2019; 10:3–19
    [Google Scholar]
  12. Keating LA, Wheeler PR, Mansoor H, Inwald JK, Dale J et al. The pyruvate requirement of some members of the Mycobacterium tuberculosis complex is due to an inactive pyruvate kinase: Implications for in vivo growth. Mol Microbiol 2005; 56:163–174 [View Article] [PubMed]
    [Google Scholar]
  13. Ramakrishnan T, Murthy PS, Gopinathan KP. Intermediary metabolism of Mycobacteria. Bacteriol Rev 1972; 36:65–108 [View Article]
    [Google Scholar]
  14. Edson NL. The intermediary metabolism of the Mycobacteria. Bacteriol Rev 1951; 15:147–182 [View Article] [PubMed]
    [Google Scholar]
  15. Ratledge C. The physiology of the mycobacteria. Adv Microb Physiol 1976; 13:115–244 [View Article]
    [Google Scholar]
  16. Choudhary E, Thakur P, Pareek M, Agarwal N. Gene silencing by CRISPR interference in mycobacteria. Nat Commun 2015; 6:6267 [View Article] [PubMed]
    [Google Scholar]
  17. Bhawsinghka N, Dutta A, Mukhopadhyay J, Das Gupta SK. A transcriptomic analysis of the mycobacteriophage D29 genome reveals the presence of novel stoperator-associated promoters in its right arm. Microbiology (Reading) 2018; 164:1168–1179 [View Article] [PubMed]
    [Google Scholar]
  18. Samaddar S, Grewal RK, Sinha S, Ghosh S, Roy S et al. Dynamics of mycobacteriophage-mycobacterial host interaction: Evidence for secondary mechanisms for host lethality. Appl Environ Microbiol 2016; 82:124–133 [View Article] [PubMed]
    [Google Scholar]
  19. Kumar S, Stecher G, Tamura K. Mega7: Molecular Evolutionary Genetics Analysis version 7.0 for bigger datasets. Mol Biol Evol 2016; 33:1870–1874 [View Article] [PubMed]
    [Google Scholar]
  20. Janet L, Niehaus WG, Timothy J. Larson purification and characterization of glpx-encoded fructose 1,6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli. J Bacteriol 2000; 182:5624–5627
    [Google Scholar]
  21. Bong HJ, EM K, Song SY, IJ K, JI O. Tripartite regulation of the glpFKD operon involved in glycerol catabolism by gylr, CRP, and Sigf in mycobacterium smegmatis. J Bacteriol 2019; 201:24
    [Google Scholar]
  22. Hasan MR, Rahman M, Jaques S, Purwantini E, Daniels L. Glucose 6-phosphate accumulation in mycobacteria: Implications for a novel f420-dependent anti-oxidant defense system. J Biol Chem 2010; 285:19135–19144 [View Article] [PubMed]
    [Google Scholar]
  23. Gurumurthy M, Rao M, Mukherjee T, Rao SPS, Boshoff HI et al. A novel F(420) -dependent anti-oxidant mechanism protects Mycobacterium tuberculosis against oxidative stress and bactericidal agents. Mol Microbiol 2013; 87:744–755 [View Article] [PubMed]
    [Google Scholar]
  24. Spaans SK, Weusthuis RA, van der Oost J, Kengen SWM. NADPH-generating systems in bacteria and archaea. Front Microbiol 2015; 6:742 [View Article] [PubMed]
    [Google Scholar]
  25. Jayanthi Bai N, Ramachandra Pai N, Suryanarayana Murthy P, Venkitasubhramanian TA. Pathways of glucose catabolism in mmycobacterium SMEGMATIS. Can J Microbiol 1976; 22:1374–1380
    [Google Scholar]
  26. Baughn AD, Rhee KY. Metabolomics of central carbon metabolism in Mycobacterium tuberculosis. Microbiol Spectr 2014; 2: [View Article] [PubMed]
    [Google Scholar]
  27. Niederweis M. Nutrient acquisition by mycobacteria. Microbiology (Reading) 2008; 154:679–692 [View Article] [PubMed]
    [Google Scholar]
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