Respiratory ATP synthesis: the new generation of mycobacterial drug targets?

被引：74

作者：

Bald, Dirk ^{[1
]}

Koul, Anil ^{[2
]}

机构：

[1] Vrije Univ Amsterdam, Dept Mol Cell Biol, Fac Earth & Life Sci, NL-1081 HV Amsterdam, Netherlands

[2] Tibotec NV, Dept Antimicrobial Res, Johnson & Johnson Pharmaceut Res & Dev, Beerse, Belgium

来源：

FEMS MICROBIOLOGY LETTERS | 2010年 / 308卷 / 01期

关键词：

mycobacteria; ATP synthesis; respiratory chain; dormancy; antimycobacterial drugs; MULTIDRUG-RESISTANT TUBERCULOSIS; ESCHERICHIA-COLI; IN-VITRO; SYNTHASE; SUBUNIT; R207910; GROWTH; OXIDOREDUCTASE; SMEGMATIS; MECHANISM;

D O I：

10.1111/j.1574-6968.2010.01959.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Mycobacterium tuberculosis, the causative agent of tuberculosis, poses a global health challenge due to the emergence of drug-resistant strains. Recently, bacterial energy metabolism has come into focus as a promising new target pathway for the development of antimycobacterial drugs. This review summarizes our current knowledge on mycobacterial respiratory energy conversion, in particular, during the physiologically dormant state that is associated with latent or persistent tuberculosis infections. Targeting components of respiratory ATP production, such as type-2 NADH dehydrogenase or ATP synthase, is illustrated as an emerging strategy in the development of novel drugs.

引用

页码：1 / 7

页数：7

共 54 条

[1] Drug-associated mitochondrial toxicity and its detection [J].

Amacher, DE .

CURRENT MEDICINAL CHEMISTRY, 2005, 12 (16) :1829-1839

[2] A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis [J].

Andries, K ;

Verhasselt, P ;

Guillemont, J ;

Göhlmann, HWH ;

Neefs, JM ;

Winkler, H ;

Van Gestel, J ;

Timmerman, P ;

Zhu, M ;

Lee, E ;

Williams, P ;

de Chaffoy, D ;

Huitric, E ;

Hoffner, S ;

Cambau, E ;

Truffot-Pernot, C ;

Lounis, N ;

Jarlier, V .

SCIENCE, 2005, 307 (5707) :223-227

[3] Tuberculosis - Metabolism and respiration in the absence of growth [J].

Boshoff, HIM ;

Barry, CE .

NATURE REVIEWS MICROBIOLOGY, 2005, 3 (01) :70-80

[4] THE BINDING CHANGE MECHANISM FOR ATP SYNTHASE - SOME PROBABILITIES AND POSSIBILITIES [J].

BOYER, PD .

BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1140 (03) :215-250

[5] After decades of drought, new drug possibilities flood TB pipeline [J].

Check, Erika .

NATURE MEDICINE, 2007, 13 (03) :266-266

[6] Massive gene decay in the leprosy bacillus [J].

Cole, ST ;

Eiglmeier, K ;

Parkhill, J ;

James, KD ;

Thomson, NR ;

Wheeler, PR ;

Honoré, N ;

Garnier, T ;

Churcher, C ;

Harris, D ;

Mungall, K ;

Basham, D ;

Brown, D ;

Chillingworth, T ;

Connor, R ;

Davies, RM ;

Devlin, K ;

Duthoy, S ;

Feltwell, T ;

Fraser, A ;

Hamlin, N ;

Holroyd, S ;

Hornsby, T ;

Jagels, K ;

Lacroix, C ;

Maclean, J ;

Moule, S ;

Murphy, L ;

Oliver, K ;

Quail, MA ;

Rajandream, MA ;

Rutherford, KM ;

Rutter, S ;

Seeger, K ;

Simon, S ;

Simmonds, M ;

Skelton, J ;

Squares, R ;

Squares, S ;

Stevens, K ;

Taylor, K ;

Whitehead, S ;

Woodward, JR ;

Barrell, BG .

NATURE, 2001, 409 (6823) :1007-1011

[7] Growth regulation in the mycobacterial cell [J].

Cox, Robert A. ;

Cook, Gregory M. .

CURRENT MOLECULAR MEDICINE, 2007, 7 (03) :231-245

[8] A computational model of the inhibition of Mycobacterium tuberculosis ATPase by a new drug candidate R207910 [J].

de Jonge, Marc R. ;

Koymans, Luc H. H. ;

Guillemont, Jerome E. G. ;

Koul, Anil ;

Andries, Koen .

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2007, 67 (04) :971-980

[9] The Diarylquinoline TMC207 for Multidrug-Resistant Tuberculosis [J].

Diacon, Andreas H. ;

Pym, Alexander ;

Grobusch, Martin ;

Patientia, Ramonde ;

Rustomjee, Roxana ;

Page-Shipp, Liesl ;

Pistorius, Christoffel ;

Krause, Rene ;

Bogoshi, Mampedi ;

Churchyard, Gavin ;

Venter, Amour ;

Allen, Jenny ;

Palomino, Juan Carlos ;

De Marez, Tine ;

van Heeswijk, Rolf P. G. ;

Lounis, Nacer ;

Meyvisch, Paul ;

Verbeeck, Johan ;

Parys, Wim ;

de Beule, Karel ;

Andries, Koen ;

Mc Neeley, David F. .

NEW ENGLAND JOURNAL OF MEDICINE, 2009, 360 (23) :2397-2405

[10] Proton-powered subunit rotation in single membrane-bound F0F1-ATP synthase [J].

Diez, M ;

Zimmermann, B ;

Börsch, M ;

König, M ;

Schweinberger, E ;

Steigmiller, S ;

Reuter, R ;

Felekyan, S ;

Kudryavtsev, V ;

Seidel, CAM ;

Gräber, P .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2004, 11 (02) :135-141

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