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Glycogen as Key Energy Storehouse and Possibly Responsible for Multidrug Resistance in Mycobacterium tuberculosis

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Drug Resistance in Bacteria, Fungi, Malaria, and Cancer

Abstract

Tuberculosis (TB) is a major public health problem with a high mortality rate worldwide due to Mycobacterium tuberculosis (M. tuberculosis) pathogen, claiming 9.6 million total cases were estimated in 2014 and more than 1.5 million people dead. M. tuberculosis and other pathogenic mycobacterial species produce a variety of glycogen or glycogen-associated molecules like lipoarabinomannan (LAM), trehalose monomycolate (TMM), phenolic glycolipids (PGLs), trehalose dimycolate (TDM), phosphatidylinositol-containing mannosides (PIMs), etc., that represent as major glycans present in the outermost layer of M. tuberculosis. The M. tuberculosis accumulate glycogen during harsh environmental condition, i.e. presence of reactive oxygen and nitrogen intermediates, limited nutrients availability and depletion of other essential elements required for their survival within the host. The glycosyltransferases (GTs) enzyme involves two families, glycogen transferase-3 (eukaryotes) and GTs-5 (eubacterial and archaeal), that play a major role in the regulation of glycogen metabolism. In bacteria, regulation of glycogen anabolism involves several glycogen synthase enzymes, i.e. α- d-glycogen synthase A (glgA), 1,4-α-d-glucan 6-glucosyltransferase (glgB) and glucose-1-phosphate adenylyltransferase (glgC), while catabolism involves glycogen phosphorylase (glgP) enzyme. In recent years, role of glycogen was investigated enormously in the pathogenesis of M. tuberculosis. Two major glycogen conjugates present in the cell wall of M. tuberculosis are TDM and TMM. These conjugates serve as precursors for the synthesis of mycolic acid that plays a key role in the invasion and pathogenesis of M. tuberculosis. This chapter summarizes the current updates of the presence of glycogen/glycoconjugates and their physiological role in the survival and pathogenesis mechanisms of M. tuberculosis during antagonistic conditions. Also, the chapter summarizes evidence of the putative GTs in the Mycobacterium spp.

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Abbreviations

ACP reductase:

Enoyl-acyl carrier protein reductase

ADP:

Adenosine diphosphate

AM:

Arabinomannan

CR-3:

Complement receptor 3

G1P:

Glucose-1-phosphate

G6P:

Glucose-6-phosphate

glgA:

α- d -Glycogen synthase A

glgB:

1,4-α-d-Glucan 6-glucosyltransferase

glgC :

Glucose-1-phosphate adenylyltransferase

glgP:

Glycogen phosphorylase

glgX :

Glucan hydrolase

GS:

Glycogen synthase

GTB:

Glycosyltransferase B

GTs:

Glycosyltransferases

KGD:

α-Ketoglutarate decarboxylase

LAM:

Lipoarabinomannan

LPS:

Lipopolysaccharide

M. tuberculosis :

Mycobacterium tuberculosis

MGLP:

6-O-Methylglucosyl-containing lipopolysaccharides

NPP:

Nucleotide pyrophosphate

ODHc:

2-Oxoglutarate dehydrogenase complex

PAMP:

Pathogen-associated molecular patterns

PGLs:

Phenolic glycolipids

PGM:

Phosphoglucomutase

PI:

Phosphatidyl-myo-inositol

PIMs:

Phosphatidylinositol-containing mannosides

STRE:

Cis-element stress response element

TB:

Tuberculosis

TLR2:

Toll-like receptor

TMM:

Trehalose monomycolate

UDP:

Uridine diphosphate

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  1. Division of Clinical Microbiology and Molecular Medicine, All India Institute of Medical Sciences, New Delhi, 110029, India

    Anil Kumar Gupta, Amit Singh & Sarman Singh MD, FRSC, FRSTMH, FAMS

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  1. Anil Kumar Gupta
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  2. Amit Singh
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  3. Sarman Singh MD, FRSC, FRSTMH, FAMS
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Correspondence to Sarman Singh MD, FRSC, FRSTMH, FAMS .

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  1. CSIR - Institute of Genomics and Integrative Biology, Delhi, India

    Gunjan Arora

  2. National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA

    Andaleeb Sajid

  3. CSIR - Institute of Genomics and Integrative Biology, Delhi, India

    Vipin Chandra Kalia

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© 2017 Springer International Publishing Switzerland

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Gupta, A.K., Singh, A., Singh, S. (2017). Glycogen as Key Energy Storehouse and Possibly Responsible for Multidrug Resistance in Mycobacterium tuberculosis . In: Arora, G., Sajid, A., Kalia, V. (eds) Drug Resistance in Bacteria, Fungi, Malaria, and Cancer. Springer, Cham. https://doi.org/10.1007/978-3-319-48683-3_11

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