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2018 | OriginalPaper | Buchkapitel

Glycoconjugate-Based Inhibitors of Mycobacterium Tuberculosis GlgE

verfasst von : Sri Kumar Veleti, Steven J. Sucheck

Erschienen in: Coupling and Decoupling of Diverse Molecular Units in Glycosciences

Verlag: Springer International Publishing

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Abstract

Tuberculosis (TB) is the leading cause of death globally as a result of a single infectious disease. A staggering 6 million new cases were reported in the 2014. In order to eradicate the ongoing threat of TB and combat rising rates of TB drug resistance new therapeutics must be developed. In this chapter, we briefly review the history of TB, Mycobacterium tuberculosis (Mtb) cell wall structure, the enzymes involved in synthesizing cell wall, and the trehalose utilization pathways (TUP). We focus on the recent discovery of enzyme Mtb GlgE, a glycosyl hydrolase-like phosphorylase, which has been found to be essential for Mtb viability and the ongoing efforts to design inhibitors against this target.

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Vorheriges Kapitel Recent Advances in the Stereochemical Outcome of Multicomponent Reactions Involving Convertible Isocyanides

Nächstes Kapitel Selective Transformations of the Anomeric Centre in Water Using DMC and Derivatives

Koch R (1882) Lecture on the discovery of Mycobacterium tuberculosis

World Health Organisation (2015) The Global tuberculosis report 2015. World Health Organization, Geneva

Brennan P, Young D, Robertson B (2008) Handbook of anti-tuberculosis agents. Tuberculosis 88(2):85–170CrossRef

Chiang CY, Centis R, Migliori GB (2010) Drug-resistant tuberculosis: past, present, future. Respirology 15(3):413–432CrossRef

Crofton J (1960) Tuberculosis undefeated. Brit Med J 2(5200):679CrossRef

Mitchison D (2000) Role of individual drugs in the chemotherapy of tuberculosis. Int J Tuberc Lung Dis 4(9):796–806

Udwadia ZF, Amale RA, Ajbani KK, Rodrigues C (2012) Totally drug-resistant tuberculosis in India. Clin Infect Dis 54(4):579–581CrossRef

Ginsberg A (2011) Research spotlight: The TB alliance: overcoming challenges to chart the future course of TB drug development. Future Med Chem 3(10):1247–1252CrossRef

Jones D, Metzger H, Schatz A, Waksman SA (1944) Control of gram-negative bacteria in experimental animals by streptomycin. Science 100(2588):103–105CrossRef

10.

Waksman SA, Reilly HC, Schatz A (1945) Strain specificity and production of antibiotic substances: V. strain resistance of bacteria to antibiotic substances, especially to streptomycin. P Natl Acad Sci USA 31(6):157

11.

Lehmann J (1946) Para-aminosalicylic acid in the treatment of tuberculosis. The Lancet 247(6384):15–16CrossRef

12.

Janin YL (2007) Antituberculosis drugs: ten years of research. Bioorg Med Chem 15(7):2479–2513CrossRef

13.

Zhang Y, Yew W (2009) Mechanisms of drug resistance in Mycobacterium tuberculosis [State of the art series. Drug-resistant tuberculosis. Edited by CY. Chiang. Number 1 in the series]. Intl J Tuberc Lung Dis 13(11):1320–1330

14.

Falzon D, Jaramillo E, Schünemann H, Arentz M, Bauer M, Bayona J, Blanc L, Caminero J, Daley C, Duncombe C (2011) WHO guidelines for the programmatic management of drug-resistant tuberculosis: 2011 update. Eur Respir J 38(3):516–528CrossRef

15.

Lamichhane G (2011) Novel targets in M. tuberculosis: search for new drugs. Trends Mol Med 17(1):25–33CrossRef

16.

Kalscheuer R, Syson K, Veeraraghavan U, Weinrick B, Biermann KE, Liu Z, Sacchettini JC, Besra G, Bornemann S, Jacobs WR Jr (2010) Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an [alpha]-glucan pathway. Nat Chem Biol 6(5):376–384CrossRef

17.

Daffé M, Draper P (1997) The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol 39:131–203CrossRef

18.

Barsom EK, Hatfull GF (1996) Characterization of a Mycobacterium smegmatis gene that confers resistance to phages L5 and D29 when overexpressed. Mol Microbiol 21(1):159–170CrossRef

19.

Tam P-H, Lowary TL (2009) Recent advances in mycobacterial cell wall glycan biosynthesis. Curr Opin Chem Biol 13(5):618–625CrossRef

20.

Crick DC, Mahapatra S, Brennan PJ (2001) Biosynthesis of the arabinogalactan-peptidoglycan complex of Mycobacterium tuberculosis. Glycobiology 11(9):107R–118RCrossRef

21.

Kremer L, Dover LG, Morehouse C, Hitchin P, Everett M, Morris HR, Dell A, Brennan PJ, McNeil MR, Flaherty C (2001) Galactan biosynthesis in Mycobacterium tuberculosis Identification of a bifunctional UDP-galactofuranosyltransferase. J Biol Chem 276(28): 26430–26440

22.

Alderwick L, Birch H, Mishra A, Eggeling L, Besra G (2007) Structure, function and biosynthesis of the Mycobacterium tuberculosis cell wall: arabinogalactan and lipoarabinomannan assembly with a view to discovering new drug targets. Biochem Soc T 35(5):1325–1328CrossRef

23.

Besra GS, Brennan PJ (1997) The mycobacterial cell envelope. J Pharm Pharmacol 49(S1):25–30CrossRef

24.

Dover LG, Alderwick LJ, Brown AK, Futterer K, Besra GS (2007) Regulation of cell wall synthesis and growth. Curr Mol Med 7(3):247–276CrossRef

25.

Besra GS, Khoo K-H, McNeil MR, Dell A, Morris HR, Brennan PJ (1995) A new interpretation of the structure of the mycolyl-arabinogalactan complex of Mycobacterium tuberculosis as revealed through characterization of oligoglycosylalditol fragments by fast-atom bombardment mass spectrometry and 1H nuclear magnetic resonance spectroscopy. Biochemistry 34(13):4257–4266CrossRef

26.

Kaur D, Guerin ME, Škovierová H, Brennan PJ, Jackson M (2009) Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis. Adv Appl Microbiol 69:23–78CrossRef

27.

Favrot L, Ronning DR (2012) Targeting the mycobacterial envelope for tuberculosis drug development. Expert Rev Anti Infect Ther 10(9):1023–1036CrossRef

28.

Nigou J, Gilleron M, Puzo G (2003) Lipoarabinomannans: from structure to biosynthesis. Biochimie 85(1):153–166CrossRef

29.

Kaur D, Berg S, Dinadayala P, Gicquel B, Chatterjee D, McNeil MR, Vissa VD, Crick DC, Jackson M, Brennan PJ (2006) Biosynthesis of mycobacterial lipoarabinomannan: role of a branching mannosyltransferase. P Natl Acad Sci 103(37):13664–13669CrossRef

30.

Besra GS, Morehouse CB, Rittner CM, Waechter CJ, Brennan PJ (1997) Biosynthesis of mycobacterial lipoarabinomannan. J Biol Chem 272(29):18460–18466CrossRef

31.

Mishra AK, Driessen NN, Appelmelk BJ, Besra GS (2011) Lipoarabinomannan and related glycoconjugates: structure, biogenesis and role in Mycobacterium tuberculosis physiology and host–pathogen interaction. FEMS Microbiol Rev 35(6):1126–1157CrossRef

32.

Strohmeier GR, Fenton MJ (1999) Roles of lipoarabinomannan in the pathogenesis of tuberculosis. Microbes Infect 1(9):709–717CrossRef

33.

Gaitonde V, Sucheck SJ (2015) Antitubercular drugs based on carbohydrate derivatives. carbohydrate chemistry: state of the art and challenges for drug development: an overview on structure, biological roles, synthetic methods and application as therapeutics, 441

34.

Singer MA, Lindquist S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1(5):639–648CrossRef

35.

Erdei É, Molnár M, Gyémánt G, Antal K, Emri T, Pócsi I, Nagy J (2011) Trehalose overproduction affects the stress tolerance of Kluyveromyces marxianus ambiguously. Bioresource Technol 102(14):7232–7235CrossRef

36.

Paul MJ, Primavesi LF, Jhurreea D, Zhang Y (2008) Trehalose metabolism and signaling. Annu Rev Plant Biol 59:417–441CrossRef

37.

Gavalda S, Bardou F, Laval F, Bon C, Malaga W, Chalut C, Guilhot C, Mourey L, Daffé M, Quémard A (2014) The polyketide synthase Pks13 catalyzes a novel mechanism of lipid transfer in mycobacteria. Chem Bio 21(12):1660–1669CrossRef

38.

Li W, Upadhyay A, Fontes FL, North EJ, Wang Y, Crans DC, Grzegorzewicz AE, Jones V, Franzblau SG, Lee RE (2014) Novel insights into the mechanism of inhibition of MmpL3, a target of multiple pharmacophores in Mycobacterium tuberculosis. Antimicrob Agents Chemother 58(11):6413–6423CrossRef

39.

Harth G, Lee B-Y, Wang J, Clemens DL, Horwitz MA (1996) Novel insights into the genetics, biochemistry, and immunocytochemistry of the 30-kilodalton major extracellular protein of Mycobacterium tuberculosis. Infect Immun 64(8):3038–3047

40.

Jackson M, Raynaud C, Lanéelle M A, Guilhot C, Laurent‐Winter C, Ensergueix D, Gicquel B, Daffé M Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope. Mol Microbiol 31(5):1573–1587

41.

De Smet KA, Weston A, Brown IN, Young DB, Robertson BD (2000) Three pathways for trehalose biosynthesis in mycobacteria. Microbiology 146(1):199–208CrossRef

42.

Gibson RP, Turkenburg JP, Charnock SJ, Lloyd R, Davies GJ (2002) Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem Biol 9(12):1337–1346CrossRef

43.

Cole S, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon S, Eiglmeier K, Gas S, Barry CR (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393(6685):537–544CrossRef

44.

Sassetti CM, Boyd DH, Rubin EJ (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48(1):77–84CrossRef

45.

Murphy HN, Stewart GR, Mischenko VV, Apt AS, Harris R, McAlister MS, Driscoll PC, Young DB, Robertson BD (2005) The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis. J Biol Chem 280(15):14524–14529CrossRef

46.

Kalscheuer R, Weinrick B, Veeraraghavan U, Besra GS, Jacobs WR (2010) Trehalose-recycling ABC transporter LpqY-SugA-SugB-SugC is essential for virulence of Mycobacterium tuberculosis. P Natl Acad Sci 107(50):21761–21766CrossRef

47.

Portevin D, de Sousa-D’Auria C, Houssin C, Grimaldi C, Chami M, Daffé M, Guilhot C (2004) A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms. P Natl Acad Sci 101(1):314–319CrossRef

48.

Fraga J, Maranha A, Mendes V, Pereira PJB, Empadinhas N, Macedo-Ribeiro S (2015) Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway. Sci Rep 5

49.

Kalscheuer R, Jacobs WR Jr (2010) The significance of GlgE as a new target for tuberculosis. Drug News Perspect 23(10):619–624CrossRef

50.

Syson K, Stevenson CE, Rejzek M, Fairhurst SA, Nair A, Bruton CJ, Field RA, Chater KF, Lawson DM, Bornemann S (2011) Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target. J Biol Chem 286(44):38298–38310CrossRef

51.

Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S (2014) Structural insight into how streptomyces coelicolor maltosyl transferase GlgE binds α-Maltose-1-phosphate and forms a maltosyl-enzyme intermediate. Biochemistry 53(15):2494–2504CrossRef

52.

Veleti SK, Lindenberger JJ, Ronning DR, Sucheck SJ (2014) Synthesis of a C-phosphonate mimic of maltose-1-phosphate and inhibition studies on Mycobacterium tuberculosis GlgE. Bioorg Med Chem 22(4):1404–1411CrossRef

53.

Lindenberger JJ, Veleti SK, Wilson BN, Sucheck SJ, Ronning DR (2015) Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors. Sci Rep 5

54.

Provencher L, Steensma DH, Wong C-H (1994) Five-membered ring azasugars as potent inhibitors of α-L-rhamnosidase (naringinase) from Penicillium decumbens. Bioorg Med Chem 2(11):1179–1188CrossRef

55.

de Melo EB, da Silveira Gomes A, Carvalho I (2006) α- and β-Glucosidase inhibitors: chemical structure and biological activity. Tetrahedron 62(44):10277–10302CrossRef

56.

Izquierdo I, Plaza MT, Yáñez V (2007) Polyhydroxylated pyrrolidines: synthesis from d-fructose of new tri-orthogonally protected 2, 5-dideoxy-2, 5-iminohexitols. Tetrahedron 63(6):1440–1447CrossRef

57.

Veleti SK, Lindenberger JJ, Thanna S, Ronning DR, Sucheck SJ (2014) Synthesis of a Poly-hydroxypyrolidine-Based inhibitor of Mycobacterium tuberculosis GlgE. J Org Chem 79(20):9444–9450CrossRef

58.

Thanna S, Lindenberger JJ, Gaitonde VV, Ronning DR, Sucheck SJ (2015) Synthesis of 2-deoxy-2, 2-difluoro-α-maltosyl fluoride and its X-ray structure in complex with Streptomyces coelicolor GlgEI-V279S. Org Biomol Chem 13(27):7542–7550CrossRef

59.

Veleti SK, Petit C, Ronning DR, Sucheck SJ (2016) Synthesis and inhibition studies of proline and pyrolidene-based phosphonates to inhibit Streptomyces Coelicolor (Sco) GlgE (manuscript in preparation)

60.

Sengupta S, Roy D, Bandyopadhyay S (2014) Modeling of a new tubercular maltosyl transferase, GlgE, study of its binding sites and virtual screening. Mol Biol Rep 41(6):3549–3560CrossRef

61.

Arooj M, Sakkiah S, Kim S, Arulalapperumal V, Lee KW (2013) A combination of receptor-based pharmacophore modeling & QM techniques for identification of human chymase inhibitors. PLoS One 8(4):e63030CrossRef

62.

Silverman RB, Holladay MW (2014) The organic chemistry of drug design and drug action

63.

Lipinski CA, Lombardo F, Dominy BW, Feeney PJ (2012) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 64:4–17CrossRef

64.

Cramer CJ (2013) Essentials of computational chemistry: theories and models. Wiley, New Jersey

65.

Billones JB, Valle AMF (2014) Structure-based design of inhibitors against maltosyltransferase GlgE. Orient J Chem 30(3):1137–1145CrossRef

66.

Sengupta S, Roy D, Bandyopadhyay S (2015) Structural insight into Mycobacterium tuberculosis maltosyl transferase inhibitors: pharmacophore-based virtual screening, docking, and molecular dynamics simulations. J Biomol Struct Dyn 33(12):2655–2666CrossRef

Titel: Glycoconjugate-Based Inhibitors of Mycobacterium Tuberculosis GlgE
verfasst von: Sri Kumar Veleti
Steven J. Sucheck
Verlag: Springer International Publishing
Buch: Coupling and Decoupling of Diverse Molecular Units in Glycosciences
Print ISBN: 978-3-319-65586-4

Electronic ISBN: 978-3-319-65587-1

Copyright-Jahr: 2018
DOI: https://doi.org/10.1007/978-3-319-65587-1_4