113
Views
19
CrossRef citations to date
0
Altmetric
Review

Recent advances towards identification of new drug targets for Mycobacterium tuberculosis

, &
Pages 79-93 | Published online: 02 Mar 2005

Bibliography

  • SNIDER DE Jr, RAVIGLIONE M, KOCHI A: Tuberculosis: pathogenetic, protection, and control. Bloom BR (Ed.), American Society for Microbiology, Washington DC, USA (1994):2–11.
  • KOCHI A: WHO report on the tuberculosis epidemic (1996).
  • CULLITON BJ: Drug-resistant TB may bring epidemic. Nature (1992) 356:473. Erratum 737.
  • STURGILL-KOSZYCKI S, SCHLESINGER PH, CHAKRABORTY P et al.: Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science (1994) 263:678–681.
  • ••Report elucidating inhibition of vesicular acidification as a survival strategy of M tuberculosis
  • ARMSTRONG JA, HART PD: Phagosome—lysosome interaction in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual non-fusion pattern and observation on bactericidal survival.j Exp. Med. (1975) 142:1–16.
  • NOSS EH, HARDING CV, BOOM WH: Mycobacterium tuberculosis inhibits MHC Class II antigen processing in murine bone marrow macrophages. Cell. brimunol. (2000) 201:63–74.
  • FERRARI G, LANGEN H, NAITO M, PIETERS J: A coat protein on phagosomes involved in the intracellular survival of mycobacteria. Cell (1999) 97:435–447.
  • GHOSH S, PAL S, DAS S, DASGUPTA SK, MAJUMDAR S: Lipoarabinomannan induced cytotoxic effects in human mononuclear cells. FEMS Immunol. Med. Microbial. (1998) 21:181–188.
  • ZAHRT TC: Molecular mechanisms regulating persistent Mycobacterium tuberculosis infection. Microbes Infect. (2003) 5:159–167.
  • WINDER G, COLLINS PB: Inhibition by isoniazid of synthesis of mycolic acids in Mycobacterium tuberculosis J. Gen. Microbiol (1970) 63:41–48.
  • ••A report deciphering the mechanism ofaction of INH.
  • BANERJEE A, DUBNAU E, QUEMARD A et al: inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis Science (1994) 263:227–230.
  • TELENTI A, IMBODEN P, MARCHESI F, LOWRIE D, COLE S, COLSTON MJ: Detection of rifampicin-resistance mutations in Mycobacterium tuberculosis Lancet (1993) 341:647–650.
  • ZIMHONY O, COX JS, WELCH JT, VILCHEZE C, JACOBS WR Jr: Pyrazinamide inhibits the eukaryotic-like fatty acid synthetase I (FAST) of Mycobacterium tuberculosis Nat. Med. (2000) 6:1043–1047.
  • ••A report unravelling the mechanism ofaction of PZA.
  • TAKAYAMA K, KILBURN JO: Inhibition of synthesis of arabinogalactan by ethambutol in Mycobacterium smegmatis. Antimicrob. Agents Chemother (1989) 33:1493–1499.
  • WINDER FG: The antibacterial action of streptomycin, isoniazid and PAS. In: Chemotherapy of tuberculosis Barry VC (Ed.), Butterworth & Co. Ltd, London, UK (1964):111–149.
  • ZHANG Y, TELENTI A: In: Molecular Genetics of mycobacteria. Hatfull GF, Jacobs WR Jr (Eds), ASM Press, Washington DC, USA (2000):235–254.
  • RANDO RR: On the mechanism of action of antibiotics which act as irreversible enzyme inhibitors. Biochem. Pharmacol (1975) 24:1153–1160.
  • JACOBS MR: Activity of quinolones against mycobacteria. Drugs (1995) 58:19–22.
  • GILLESPIE SH: Evolution of drug resistance in Mycobacterium tuberculosis: clinical and molecular perspective. Antimicrob. Agents Chemother: (2002) 46:267–274.
  • WORLD HEALTH ORGANIZATION: Tuberculosis Fact Sheet (No. 104) 2000.
  • SNIDER DE JR, CASTRO KG: The global threat of drug-resistant tuberculosis. N Engl. J. Med. (1998) 338:1689–1690.
  • MAHMOUDI A, ISEMAN MD: Pitfalls in the care of patients with tuberculosis. Common errors and their association with the acquisition of drug resistance. JAMA (1993) 270:65–68.
  • ZHANG Y, MARIO AL: Tuberculosis drug targets. Curr. Drug Targets (2002) 3:131–154.
  • COLE ST, BROSCH R, PARKHILL J et al: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature (1998) 393:537–544
  • ••Complete genome sequence of M tuberculosis.
  • SASSETTI CM, BOYD D H, RUBIN EJ: Genes required for mycobacterial growth defined by high-density mutagenesis. Microbiol (2003) 48:77–84.
  • BUCHMEIER N, BLANC-POTARD A, EHRT S, PIDDINGTON D, RILEY L, GROISMAN EA: A parallel intraphagosomal survival strategy shared by Mycobacterium tuberculosis and Salmonella enterica. Mol. Microbiol (2000) 35:1375–1382.
  • GOLD B, RODRIGUEZ GM, MARRAS SA, PENTECOST M, SMITH I: The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Mol Mier-chid. (2001) 42:851–865.
  • DE VOSS JJ, RUTTER K, SCHROEDER BG, SU H, ZHU Y, BARRY CE III: The salicylate-derived mycobactein siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc. Natl. Acad. Sci. USA (2000) 97:1252–1257.
  • •Report indicating the importance of iron uptake in the survival of M tuberculosis.
  • HONDALUS MK, BARDAROV S, RUSSELL R, CHAN J, JACOBS WR Jr, BLOOM BR: Attenuation of and protection induced by a leucine auxotroph of Mycobacterium tuberculosis. Infect. Inman. (2000) 68:2888–2898.
  • PAVELKA MS Jr, CHEN B, KELLEY CL, COLLINS FM, JACOBS WR Jr: Vaccine efficacy of a lysine auxotroph of Mycobacterium tuberculosis. Infect. Inman. (2003) 71:4190–4192.
  • SMITH DA, PARISH T, STOKER NG, BANCROFT GJ: Characterization of auxotrophic mutants of Mycobacterium tuberculosis and their potential as vaccine candidates. Infect. Inman. (2001) 69:1142–1150.
  • JACKSON M, PHALEN SW, LAGRANDERIE M et al.: Persistence and protective efficacy of a Mycobacterium tuberculosis auxotroph vaccine. Infect. Inman. (1999) 67:2867–2873.
  • PEREIRA JH, CANDURI F, DE OLIVEIRA JS, DA SILVEIRA NJ, BASSO LA, PALMA MS: Structural bioinformatics study of EPSP synthase from Mycobacterium tuberculosis. Biochem. Biophys. Res. Commun. (2003) 312:608–614.
  • SAMBANDAMURTHY VK, WANG X, CHEN B et al: A pantothenate auxotrophs of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis. Nat. Med. (2002) 8:1171–1174.
  • •This report highlights the importance of pantothenate biosynthesis in the pathogenesis of M tuberculosis
  • HUOVINEN P, SUNDSTROM L, SWEDBERG G, SKOLD O: Trimethoprim and sulfonamide resistance. Antimicrob. Agents Chemother. (1995) 39:279–289.
  • LOCHER HH, SCHLUNEGGER H, HARTMAN PG, ANGEHRN P, THEN RL: Antibacterial activities of epiroprim, a new dihydrofolate reductase inhibitor, alone and in combination with dapsone. Antimicrob. Agents Chemother: (1996) 40:1376–1381.
  • GLICKMANN MS: A novel mycolic acidcyclopropane synthetase is required for cording, persistance and virulence of Mycobacterium tuberculosis. Ma Cell. (2000) 5:717–727.
  • MCKINNEY JD, HONER ZU BENTRUP K, MUNOZ-ELIAS EJ et al.: Persistance of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature (2000) 406:735–738.
  • ••The importance of isocitrate lyase in themycobacterial persistence and virulence was illustrated.
  • RAYNAUD C, GUILHOT C, RAUZIER Jet al.: Phospholipases C are involved in the virulence of Mycobacterium tuberculosis. Ma Microbic] (2002) 45:203–217.
  • BOSHOFF HI, REED MB, BARRY CE III, MIZRAHI V: DnaE2 polymerase contributes to M vivo survival and the emergence of drug resistance in Mycobacterium tuberculosis Cell (2003) 113:183–193.
  • ••A recent report showing the importance ofincreased mutation rates in the generation of more fit' mycobacterial strains.
  • DAHL JL, KRAUS CN, BOSHOFF HI et al.: The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Proc. Nat] Acad. Sci. USA (2003) 100:10026–10031.
  • SUN Z, ZHANG Y: Spent culture supernatant of Mycobacterium tuberculosis H37Ra improves viability of aged cultures of this strain and allows small inocula to initiate growth. Bacteria (1999) 181:7626–7628.
  • ZHANG Y, YANG Y, WOODS A et al.:Resuscitation of dormant Mycobacterium tuberculosis by phospholipids or specific peptides. Biochem. Biophys. Res. Commun. (2001) 284:542–547.
  • MUKAMOLOVA GV, KAPRELYANTS AS, YOUNG DI et at A bacterial cytokine. Proc. Natl. Acad. Sri. USA (1998) 95:8916–8921.
  • CHOPRA P, MEENA LS, SINGH Y: New drug targets of Mycobacterium tuberculosis. Indian Med. Res. (2003) 117:1–9.
  • COHEN P: Protein kinases - the major drug targets of the twenty-first century? Nat. Rev Drug Discov (2002) 1:309–315.
  • LYON MA, DUCRUET AP, WIPE P, LAZO JS: Dual-specificity phosphatases as targets for antineoplastic agents. Nat. Rev Drug Discov. (2002) 1:961–976.
  • VAN HUIJSDUIJNEN RH, BOMBRUN A, SWINNEN D: Selecting protein tyrosine phosphatases as drug targets. Drug Discov. Today (2002) 7:1013–1019.
  • MCCLUSKEY A, SAKOFF JA: Small molecule inhibitors of serine/ threonine protein phosphatases. Mini Rev Med. Chem. (2001) 1:43–55.
  • HUIJSDUIJNEN RHV, BOMBRUN A, SWINNEN D: Selecting protein tyrosine phosphatases as drug targets. Drug Discov. Today (2002) 7:1013–1019.
  • PATHAK MK, YI T: Sodium stibogluconate is a potent inhibitor of protein tyrosine phosphatases and augments cytokine responses in hemopoietic cell lines. .1. Immuna (2001) 167:3391–3397.
  • AV-GAY Y, EVERETT M: The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbia (2000) 8:234–244.
  • HAKANSSON SE, GALYOV EE, ROSQVIST R, WOLF-WATZ H: The Yersinia YpIcA Ser/Thr kinase is translocated into and subsequently targeted to the inner surface of the Hela cell plasma membrane. Ma. Microbia (1996) 20:593–603.
  • •Study indicating the importance of eukaryotic-type serine/threonine kinase in the bacterial pathogenesis.
  • DREWS S J, HUNG F, AV-GAY Y: A protein kinase inhibitor as an antibacterial agent. FEMS Microbia Lett. (2001) 205:369–374.
  • CHABA R, RAJE M, CHAKRABARTY PK:Evidences that a eukaryotic-type serine/ threonine protein kinase from Mycobacterium tuberculosisregulates morphological changes associated with cell division. Eur. I Biochent. (2002) 269:1078–1085.
  • ORTIZ-LOMBARDIA M, POMPEO F, BOITEL B, ALZARI PM: Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis I Biol. Chem. (2003) 278:13094–13100.
  • YOUNG TA, DELAGOUTTE B, ENDRIZZI JA, FALICK AM, ALBERT: Structure of Mycobaterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. (2003) 10:168–174.
  • AV-GAY Y, JAMIL S, DREWS SJ: Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB. Infect. Immun. (1999) 67:5676–5682.
  • KOUL A, CHOIDAS A, TYAGI AK et al.:Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization. Microbiology(2001) 147:2307–2314.
  • SHARMA K, CHANDRA H, GUPTA PK et al.: PknH, a transmembrane Hank's type serine/threonine kinase from Mycobacterium tuberculosis is differentially expressed under stress conditions. FEMS Microbia Lett. (2004). In Press.
  • MOLLE V, KREMER L, GIRARD-BLANC C, BESRA GS, COZZONE AJ, PROST JF: An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis. Biochemistry (Mosc) (2003) 42:15300–15309.
  • COWLEY SC, AV-GAY Y: Promoter activity and protein localization in Mycobacterium spp. using green fluorescent protein. Gene (2001) 264:225–231.
  • AGARWAL N, TYAGI AK: Role of 5 --TGN-3 motif in the interaction of mycobacterial RNA polymerase with a promoter of 'extended-10' class. FEMS Microbia Lett. (2003) 225:75–83.
  • BERT KLEBL: Target driven drug discovery in TB, employing the mycobacterial kinase PknG. Gordon Research Conference on Tuberculosis Drug Discovery. Oxford, UK (2003).
  • FU Y, GALAN JE: A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host cell recovery after bacterial invasion. Nature (1999) 401:293–297.
  • BLISKA JB, GUAN K, DIXON JE, FALKOW S: Tyrosine phosphatase hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc. Natl. Acad. Sci USA (1991) 88:1187–1191.
  • KUSNER DJ, HALL CE SCHLESINGER LS: Activation of phospholipase D is tightly coupled to the phagocytosis of Mycobacterium tuberculosis or opsonized zymosan by human macrophages. Exp. Med. (1996) 184:585–595.
  • DE CAMILLI P, EMR SD, MCPHERSON PS, NOVICK P: Phosphoinositides as regulators of membrane traffic. Sdence (1996) 271:1533–1539.
  • MALIK ZA, THOMPSON CR, HASHIMI S, PORTER B, IYER SS, KUSNER DJ: Cutting edge: Mycobacterium tuberculosis blocks Ca2' signaling and phagosome maturation in human macrophages via specific inhibition of sphingosine kinase. Immunol. (2003) 170:2811–2815.
  • HESTVIK AL, HMAMA Z, AV-GAY Y: Kinome analysis of host response to mycobacterial infection: a novel technique in proteomics. Infect. Immun. (2003) 71:5514–5522.
  • VERGNE I, CHUA J, DERETIC V: Tuberculosis toxin blocking phagosome maturation inhibits a novel Ca2V calmodulin-PI3K hVPS34 cascade. Exp. Med. (2003) 198:653–659.
  • SINGH B, SINGH G, TRAJKOVIC V, SHARMA P: Intracellular expression of Mycobacterium tuberculosis-specific 10-kDa antigen down-regulates macrophage B7.1 expression and nitric oxide release. Clin. Exp. Immuna (2003) 134:70–77.
  • KOUL A, CHOIDAS A, TREDER M et al.: Cloning and characterization of secretory tyrosine phosphatase of Mycobacterium tuberculosis Bacterioi (2000) 182:5425–5432.
  • SINGH R, RAO V, SHAKILA H et al.: Disruption of mptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs. Ma Microbial. (2003) 50:751–762.
  • ••First study unveiling the importance oftyrosine phosphatase in the virulence of M tuberculosis
  • COWLEY SC, BABAKAIFF R, AV-GAY Y:Expression and localization of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA. Res. Microbial. (2002) 153:233–241.
  • CHOPRA P, SINGH B, SINGH R et al.: Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates serine-threonine kinases PknA and PknB. Biochem. Biophys. Res. Commun. (2003) 311:112–120.
  • BOITEL B, ORTIZ-LOMBARDIA M, DURAN R et al.: PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis. Ma Microbia (2003) 49:1493–1508.
  • HOCH JA: Two-component and phosphorelay signal transduction. Curr. Opin. Microbial. (2000) 3:165–170.
  • PARISH T, SMITH DA, KENDALL S, CASALI N, BANCROFT GJ, STOKER NG: Deletion of two-component regulatory systems increases the virulence of Mycobacterium tuberculosis. Infect. Immun. (2003) 71:1134–1140.
  • PEREZ E, SAMPER S, BORDAS Y, GUILHOT C, GICQUEL B, MARTIN C: An essential role for phoP in Mycobacterium tuberculosis virulence. Ma Microbia (2001) 41:179–187.
  • ZAHRT TC, DERETIC V: An essential two-component signal transduction system in Mycobacterium tuberculosis. Bacteria (2000) 182:3832–3838.
  • DASGUPTA N, KAPUR V, SINGH KK et al.: Characterization of a two-component system, devR-devS, of Mycobacterium tuberculosis Tuber. Lung Dis. (2000) 80:141–159.
  • GLICKMAN MS, JACOBS WB Jr: Microbial pathogenesis of Mycobacterium tuberculosis; dawn of a discipline. Cell (2001) 104:477–485.
  • NIEDERWEIS M: Mycobacterial porins - new channel proteins in unique outer membranes. Ma Microbial. (2003) 49:1167–1177.
  • DEVERGNE O, EMILIE D, PEUCHMAUR M, CREVON MC, DIAGAY MF, GALANAUD P: Production of cytokines in sarcoid lymph nodes: preferential expression of interleukin-1-13 and interferon-y genes. Hum. Patha (1992) 23:317–323.
  • CHAN J, RAN X, HUNTER SW, BRENNAN PJ, BLOOM BR: Lipoarabinomannan, a possible virulence factor involved in persistence of Mycobacterium tuberculosis within macrophages. Infect. Inman. (1991) 59:1755–1761.
  • BERTHET FX, LAGRANDERIE M, GOUNON P et al.: Attenuation of virulence by disruption of the Mycobacterium tuberculosis erp gene. Science (1998) 282:759–762.
  • COX JS, CHEN B, MCNEIL M, JACOBS WR Jr: Complex lipid determines tissue specific replication of Mycobacterium tuberculosis in mice. Nature (1999) 402:79–83.
  • DUBNAU E, CHAN J, RAYNAUD C et al.: Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice. Ma Microbial. (2000) 36:630–637.
  • MAY, STERN RJ, SCHERMAN MS et al.: Drug targeting Mycobacterium tuberculosis cell wall synthesis: genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose. Antimicrob. Agents Chemother. (2001) 45:1407–1416.
  • HOU JY, GRAHAM JE, CLARK-CURTISS JE: Mycobacterium avium genes expressed during growth in human macrophages detected by selective capture of transcribed sequences (SCOTS). Infect. Immun. (2002) 70:3714–3726.
  • CHAKRABARTY AM: Nucleoside diphosphate kinase: role in bacterial growth, virulence, cell signalling and polysaccharide synthesis. Ma Microbia (1998) 28:875–882.
  • CHOPRA P, SINGH A, KOUL A et al.: Cytotoxic activity of nucleoside diphosphate kinase secreted from Mycobacterium tuberculosis. Eur.j Biochem. (2003) 270:625–634.
  • COLLINS DM, KAWAKAMI RP, DE LISLE GW, PASCOPELLA L, BLOOM BR, JACOBS WR Jr: Mutation of the principal 6 factor causes loss of virulence in a strain of the Mycobacterium tuberculosis complex. Proc. Nati Acad. Sci. USA (1995) 92:8036–8040.
  • ••Report showing the significance ofmycobacterial 6 factor in their virulence.
  • STEYN AJ, COLLINS DM, HONDALUS MK, JACOBS WR Jr, KAWAKAMI RP, BLOOM BR: Mycobacterium tuberculosis WhiB3 interacts with RpoV to affect host survival but is dispensable for in vivo growth. Proc. Nati Acad. Sci. USA (2002) 99:3147–3152.
  • CHEN P, RAFAEL E, RUIZ QING LI, RICHARD FS, BISHAI WR: Construction and characterization of a Mycobacterium tuberculosis mutant lacking the alternate 6 factor gene, sigE Infect. Inman. (2000) 68:5575–5580.
  • DOUKHAN L, PREDICH M, NAIR G et al.: Genomic organization of the mycobacterial 6 gene cluster. Gene (1995) 165:67–70.
  • WU QL, KONG D, LAM K, HUSSON RN: A mycobacterial extracytoplasmic function 6 factor involved in survival following stress. Bacteria (1997) 179:2922–2929.
  • RAMAN S, SONG T, PUYANG X, BARDAROV S, JACOBS WR Jr, HUSSON RN: The alternative 6 factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis. Bacteria (2001) 183:6119–6125.
  • SAREEN D, NEWTON GL, FAHEY RC, BUCHMEIER NA: Mycothiol is essential for growth of Mycobacterium tuberculosis Erdman. Bacteria (2003) 185:6736–6740.
  • BANU S, HONORE N, SAINT-JOANIS B, PHILPOTT D, PREVOST MC, COLE ST: Are the PE-PGRS proteins of Mycobacterium tuberculosis variable surface antigens? Ma Microbia (2002) 44:9–19.
  • BRENNAN MJ, DELOGU G, CHEN Y et al.: Evidence that mycobacterial PE-PGRS proteins are cell surface constituents that influence interactions with other cells. Infect. Immun. (2001) 69:7326–7333.
  • DELOGU G, BRENNAN MJ: Comparative immune response to PE and PE-PGRS antigens of Mycobacterium tuberculosis. Infect. Immun. (2001) 69:5606–5611.
  • SINGH KK, ZHANG X, PATIBANDLA AS, CHIEN P Jr, LAAL S: Antigens of Mycobacterium tuberculosis expressed during preclinical tuberculosis: serological immunodominance of proteins with repetitive amino acid sequences. Infect. Immun. (2001) 69:4185–4191.
  • RAMAKRISHNAN L, FEDERSPIEL NA, FALKO WS: Granuloma-specific expression of Mycobacterium virulence proteins from the glycine-rich PE-PGRS family. Science (2000) 288:1436-1439. First report establishing a direct role of some PE-PGRS proteins in the virulence of M tuberculosis.
  • COLE ST: Learning from the genome sequence of Mycobacterium tuberculosis H37Rv. FEBS Lett. (1999) 452:7–10.
  • FLORES J, ESPITIA C: Differential expression of PE and PE-PGRS genes in Mycobacterium tuberculosis strains. Gene (2003) 318:75–81.
  • LI Z, KELLEY C, COLLINS F, ROUSE D, MORRIS S: Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs. Infect. Dis. (1998) 177:1030–1035.
  • EDWARDS KM, CYNAMON MH, VOLADRI RK et al: Iron-cofactored superoxide dismutase inhibits host responses to Mycobacterium tuberculosis. Respit: Crit. Care Med. (2001) 164:2213–2219.
  • SKJOT RLV, OETTINGER T, ROSWNKRANDS I et al: Comparative evaluation of low-molecular-mass proteins from Mycobacterium tuberculosis identifies members of the ESAT-6 family as immunodominant T-cell antigens. Infect. Immun. (2000) 68:214–220.
  • WARDS BJ, DE LISLE GW, COLLINS DM: An esat6 knockout mutant of Mycobacterium bovis produced by homologous recombination will contribute to the development of a live tuberculosis vaccine. Tuber. Lung D (2000) 80:185–189.
  • COPP BR: Antimycobacterial natural products: Nat. Prod. Rep. (2003) 20:535–557.
  • NEWTON SM, LAU C, WRIGHT CW: A review of antimycobacterial natural products. Phytother. Res. (2000) 14:303–322.
  • NCAYIYANA DJ: Africa can solve its own health problems. Br. Med. (2002) 324:688–689.

Websites

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.