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2. Economic evaluation of shortened, bedaquiline-containing treatment regimens for rifampicin-resistant tuberculosis (STREAM stage 2): a within-trial analysis of a randomised controlled trial

Author

Ahmad, Saleem, Alexandru, Sofia, Bellenger, Katharine, Bulga, Tolera G., Cook, Claire, Crudu, Valeriu, Deborah, Bennet, Dodds, Wendy, Gebreegziabher, Belay A., Goodall, Ruth L., Gupta, Pritti, Gurumurthy, Meera, Langley, Ivor, Nalunjogi, Joanitah, Khan, Saleem, Krishnan, Saravanan, Kumar, Shravan, Lesosky, Maia, Macari, Mariana, Makwana, Mukesh, Murphy, Brendan, Murugesan, Ramesh P., Patel, Vanita, Pirlog, Irina, Rauchenberger, Mary, Sanders, Karen, Singh, Ramesh, Subramani, Sangeetha, Teferi, Mekonnen, Tegegn, Netsanet A., Velmurugan, Arun Babu, Whitney, Johanna, Rosu, Laura, Madan, Jason J, Tomeny, Ewan M, Muniyandi, Malaisamy, Nidoi, Jasper, Girma, Mamo, Vilc, Valentina, Bindroo, Priyanka, Dhandhukiya, Rajdeep, Bayissa, Adamu K, Meressa, Daniel, Narendran, Gopalan, Solanki, Rajesh, Bhatnagar, Anuj K, Tudor, Elena, Kirenga, Bruce, Meredith, Sarah K, Nunn, Andrew J, Bronson, Gay, Rusen, I D, Squire, S Bertel, and Worrall, Eve

Published
2023
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3. Evaluation of two short standardised regimens for the treatment of rifampicin-resistant tuberculosis (STREAM stage 2): an open-label, multicentre, randomised, non-inferiority trial

Author

Adilaa, Oyunchimeg, Alexandru, Sofia, Bellenger, Katharine, Bennet, Jaclyn, Bennet, Deborah, Bindroo, Priyanka, Borisagar, Ghanshyam, Cook, Claire, Dalai, Doljinsuren, Davis, Andrew, de Jong, Bouke, Dodds, Wendy, Duckworth, Lynette, Gahima, Nonhlanhla, Gebreegziabher, Belay, Goldfeld, Anne, Hanifa, Mahmud, Hughes, Gareth, Kimuli, Ivan, Komrska, Jan, Lomtadze, Nino, Murphy, Brendan, Mwelase, Thando, Nalunjogi, Joanitah, Patel, Leena, Pirlog, Irina, Qawiy, Ishmael, Rauchenberger, Mary, Rigouts, Leen, Roach, Carol, Rosu, Laura, Santos-Filho, Ezio, Senguttuvan, Thirumaran, Sisay, Million, Sridhar, Rathinam, Srinivasulu, Vignes, Teferi, Mekonnen, Teklu, Helen, Tsegeen, Narangarav, van Amsterdam, Odette, White, Lisa, Whitney, Johanna, Zagd, Chuluunbaatar, Goodall, Ruth L, Meredith, Sarah K, Nunn, Andrew J, Bayissa, Adamu, Bhatnagar, Anuj K, Bronson, Gay, Chiang, Chen-Yuan, Conradie, Francesca, Gurumurthy, Meera, Kirenga, Bruce, Kiria, Nana, Meressa, Daniel, Moodliar, Ronelle, Narendran, Gopalan, Ngubane, Nosipho, Rassool, Mohammed, Sanders, Karen, Solanki, Rajesh, Squire, S Bertel, Torrea, Gabriela, Tsogt, Bazarragchaa, Tudor, Elena, Van Deun, Armand, and Rusen, I D

Published
2022
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6. Economic evaluation of shortened, bedaquiline-containing treatment regimens for rifampicin-resistant tuberculosis (STREAM stage 2): a within-trial analysis of a randomised controlled trial

Author

Rosu, Laura, primary, Madan, Jason J, additional, Tomeny, Ewan M, additional, Muniyandi, Malaisamy, additional, Nidoi, Jasper, additional, Girma, Mamo, additional, Vilc, Valentina, additional, Bindroo, Priyanka, additional, Dhandhukiya, Rajdeep, additional, Bayissa, Adamu K, additional, Meressa, Daniel, additional, Narendran, Gopalan, additional, Solanki, Rajesh, additional, Bhatnagar, Anuj K, additional, Tudor, Elena, additional, Kirenga, Bruce, additional, Meredith, Sarah K, additional, Nunn, Andrew J, additional, Bronson, Gay, additional, Rusen, I D, additional, Squire, S Bertel, additional, Worrall, Eve, additional, Ahmad, Saleem, additional, Alexandru, Sofia, additional, Bellenger, Katharine, additional, Bulga, Tolera G., additional, Cook, Claire, additional, Crudu, Valeriu, additional, Deborah, Bennet, additional, Dodds, Wendy, additional, Gebreegziabher, Belay A., additional, Goodall, Ruth L., additional, Gupta, Pritti, additional, Gurumurthy, Meera, additional, Langley, Ivor, additional, Nalunjogi, Joanitah, additional, Khan, Saleem, additional, Krishnan, Saravanan, additional, Kumar, Shravan, additional, Lesosky, Maia, additional, Macari, Mariana, additional, Makwana, Mukesh, additional, Murphy, Brendan, additional, Murugesan, Ramesh P., additional, Patel, Vanita, additional, Pirlog, Irina, additional, Rauchenberger, Mary, additional, Sanders, Karen, additional, Singh, Ramesh, additional, Subramani, Sangeetha, additional, Teferi, Mekonnen, additional, Tegegn, Netsanet A., additional, Velmurugan, Arun Babu, additional, and Whitney, Johanna, additional

Published
2023
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7. Evaluation of two short standardised regimens for the treatment of rifampicin-resistant tuberculosis (STREAM stage 2): an open-label, multicentre, randomised, non-inferiority trial

Author

Goodall, Ruth L, primary, Meredith, Sarah K, additional, Nunn, Andrew J, additional, Bayissa, Adamu, additional, Bhatnagar, Anuj K, additional, Bronson, Gay, additional, Chiang, Chen-Yuan, additional, Conradie, Francesca, additional, Gurumurthy, Meera, additional, Kirenga, Bruce, additional, Kiria, Nana, additional, Meressa, Daniel, additional, Moodliar, Ronelle, additional, Narendran, Gopalan, additional, Ngubane, Nosipho, additional, Rassool, Mohammed, additional, Sanders, Karen, additional, Solanki, Rajesh, additional, Squire, S Bertel, additional, Torrea, Gabriela, additional, Tsogt, Bazarragchaa, additional, Tudor, Elena, additional, Van Deun, Armand, additional, Rusen, I D, additional, Adilaa, Oyunchimeg, additional, Alexandru, Sofia, additional, Bellenger, Katharine, additional, Bennet, Jaclyn, additional, Bennet, Deborah, additional, Bindroo, Priyanka, additional, Borisagar, Ghanshyam, additional, Cook, Claire, additional, Dalai, Doljinsuren, additional, Davis, Andrew, additional, de Jong, Bouke, additional, Dodds, Wendy, additional, Duckworth, Lynette, additional, Gahima, Nonhlanhla, additional, Gebreegziabher, Belay, additional, Goldfeld, Anne, additional, Hanifa, Mahmud, additional, Hughes, Gareth, additional, Kimuli, Ivan, additional, Komrska, Jan, additional, Lomtadze, Nino, additional, Murphy, Brendan, additional, Mwelase, Thando, additional, Nalunjogi, Joanitah, additional, Patel, Leena, additional, Pirlog, Irina, additional, Qawiy, Ishmael, additional, Rauchenberger, Mary, additional, Rigouts, Leen, additional, Roach, Carol, additional, Rosu, Laura, additional, Santos-Filho, Ezio, additional, Senguttuvan, Thirumaran, additional, Sisay, Million, additional, Sridhar, Rathinam, additional, Srinivasulu, Vignes, additional, Teferi, Mekonnen, additional, Teklu, Helen, additional, Tsegeen, Narangarav, additional, van Amsterdam, Odette, additional, White, Lisa, additional, Whitney, Johanna, additional, and Zagd, Chuluunbaatar, additional

Published
2022
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14. Coadministration of Allopurinol To Increase Antimycobacterial Efficacy of Pyrazinamide as Evaluated in a Whole-Blood Bactericidal Activity Model

Author

Naftalin, Claire M., primary, Verma, Rupangi, additional, Gurumurthy, Meera, additional, Lu, Qingshu, additional, Zimmerman, Matthew, additional, Yeo, Benjamin Chaik Meng, additional, Tan, Kin Hup, additional, Lin, Wenwei, additional, Yu, Buduo, additional, Dartois, Véronique, additional, and Paton, Nicholas I., additional

Published
2017
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15. A novel F420-dependent anti-oxidant mechanism protects Mycobacterium tuberculosis against oxidative stress and bactericidal agents

Author

Gurumurthy, Meera, Rao, Martin, Mukherjee, Tathagata, Rao, Srinivasa P S, Boshoff, Helena I, Dick, Thomas, Barry, Clifton E, and Manjunatha, Ujjini H

Subjects
Oxidative Stress, Bacterial Proteins, Coenzymes, NAD(P)H Dehydrogenase (Quinone), Mycobacterium tuberculosis, NAD, Research Articles, Antioxidants, Anti-Bacterial Agents
Abstract

Mycobacterium tuberculosis (Mtb) is an aerobic bacterium that persists intracellularly in host macrophages and has evolved diverse mechanisms to combat and survive oxidative stress. Here we show a novel F(420) -dependent anti-oxidant mechanism that protects Mtb against oxidative stress. Inactivation of the fbiC gene in Mtb results in a cofactor F(420) -deficient mutant that is hypersensitive to oxidative stress and exhibits a reduction in NADH/NAD(+) ratios upon treatment with menadione. In agreement with the recent hypothesis on oxidative stress being an important component of the pathway resulting in cell death by bactericidal agents, F(420) (-) mutants are hypersensitive to mycobactericidal agents such as isoniazid, moxifloxacin and clofazimine that elevate oxidative stress. The Mtb deazaflavin-dependent nitroreductase (Ddn) and its two homologues Rv1261c and Rv1558 encode for an F(420) H(2) -dependent quinone reductase (Fqr) function leading to dihydroquinones. We hypothesize that Fqr proteins catalyse an F(420) H(2) -specific obligate two-electron reduction of endogenous quinones, thereby competing with the one-electron reduction pathway and preventing the formation of harmful cytotoxic semiquinones, thus protecting mycobacteria against oxidative stress and bactericidal agents. These findings open up an avenue for the inhibition of the F(420) biosynthesis pathway or Fqr-class proteins as a mechanism to potentiate the action of bactericidal agents.

Published
2012

16. Activity of faropenem with and without rifampicin against Mycobacterium tuberculosis: evaluation in a whole-blood bactericidal activity trial

Author

Gurumurthy, Meera, primary, Verma, Rupangi, additional, Naftalin, Claire M., additional, Hee, Kim Hor, additional, Lu, Qingshu, additional, Tan, Kin Hup, additional, Issac, Simi, additional, Lin, Wenwei, additional, Tan, Angelia, additional, Seng, Kok-Yong, additional, Lee, Lawrence Soon-U., additional, and Paton, Nicholas I., additional

Published
2017
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17. Pharmacokinetics-Pharmacodynamics Analysis of Bicyclic 4-Nitroimidazole Analogs in a Murine Model of Tuberculosis

Author

Lakshminarayana, Suresh B., primary, Boshoff, Helena I. M., additional, Cherian, Joseph, additional, Ravindran, Sindhu, additional, Goh, Anne, additional, Jiricek, Jan, additional, Nanjundappa, Mahesh, additional, Nayyar, Amit, additional, Gurumurthy, Meera, additional, Singh, Ramandeep, additional, Dick, Thomas, additional, Blasco, Francesca, additional, Barry, Clifton E., additional, Ho, Paul C., additional, and Manjunatha, Ujjini H., additional

Published
2014
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19. Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824

Author

Cellitti, Susan E., primary, Shaffer, Jennifer, additional, Jones, David H., additional, Mukherjee, Tathagata, additional, Gurumurthy, Meera, additional, Bursulaya, Badry, additional, Boshoff, Helena I., additional, Choi, Inhee, additional, Nayyar, Amit, additional, Lee, Yong Sok, additional, Cherian, Joseph, additional, Niyomrattanakit, Pornwaratt, additional, Dick, Thomas, additional, Manjunatha, Ujjini H., additional, Barry, Clifton E., additional, Spraggon, Glen, additional, and Geierstanger, Bernhard H., additional

Published
2013
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22. Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824

Author

Cellitti, Susan E., primary, Shaffer, Jennifer, additional, Jones, David H., additional, Mukherjee, Tathagata, additional, Gurumurthy, Meera, additional, Bursulaya, Badry, additional, Boshoff, Helena I., additional, Choi, Inhee, additional, Nayyar, Amit, additional, Lee, Yong Sok, additional, Cherian, Joseph, additional, Niyomrattanakit, Pornwaratt, additional, Dick, Thomas, additional, Manjunatha, Ujjini H., additional, Barry, Clifton E., additional, Spraggon, Glen, additional, and Geierstanger, Bernhard H., additional

Published
2012
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23. Substrate specificity of the deazaflavin-dependent nitroreductase from Mycobacterium tuberculosis responsible for the bioreductive activation of bicyclic nitroimidazoles

Author

Gurumurthy, Meera, primary, Mukherjee, Tathagata, additional, Dowd, Cynthia S., additional, Singh, Ramandeep, additional, Niyomrattanakit, Pornwaratt, additional, Tay, Jo Ann, additional, Nayyar, Amit, additional, Lee, Yong Sok, additional, Cherian, Joseph, additional, Boshoff, Helena I., additional, Dick, Thomas, additional, Barry, Clifton E., additional, and Manjunatha, Ujjini H., additional

Published
2011
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28. A novel F420-dependent anti-oxidant mechanism protects Mycobacterium tuberculosis against oxidative stress and bactericidal agents.

Author

Gurumurthy, Meera, Rao, Martin, Mukherjee, Tathagata, Rao, Srinivasa P. S., Boshoff, Helena I., Dick, Thomas, Barry, Clifton E., and Manjunatha, Ujjini H.

Subjects
*MYCOBACTERIUM tuberculosis, *MACROPHAGES, *OXIDATIVE stress, *BACTERICIDAL action, *ANTINEOPLASTIC agents
Abstract

Mycobacterium tuberculosis ( Mtb) is an aerobic bacterium that persists intracellularly in host macrophages and has evolved diverse mechanisms to combat and survive oxidative stress. Here we show a novel F420-dependent anti-oxidant mechanism that protects Mtb against oxidative stress. Inactivation of the fbiC gene in Mtb results in a cofactor F420-deficient mutant that is hypersensitive to oxidative stress and exhibits a reduction in NADH/ NAD+ ratios upon treatment with menadione. In agreement with the recent hypothesis on oxidative stress being an important component of the pathway resulting in cell death by bactericidal agents, F420− mutants are hypersensitive to mycobactericidal agents such as isoniazid, moxifloxacin and clofazimine that elevate oxidative stress. The Mtb deazaflavin-dependent nitroreductase ( Ddn) and its two homologues Rv1261c and Rv1558 encode for an F420H2-dependent quinone reductase ( Fqr) function leading to dihydroquinones. We hypothesize that Fqr proteins catalyse an F420H2-specific obligate two-electron reduction of endogenous quinones, thereby competing with the one-electron reduction pathway and preventing the formation of harmful cytotoxic semiquinones, thus protecting mycobacteria against oxidative stress and bactericidal agents. These findings open up an avenue for the inhibition of the F420 biosynthesis pathway or Fqr-class proteins as a mechanism to potentiate the action of bactericidal agents. [ABSTRACT FROM AUTHOR]

Published
2013
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29. Identification of HEXIM1 as a Positive Regulator of p53.

Author

Qiao Jing Lew, Yi Ling Chia, Kai Ling Chu, Yuen Ting Lam, Gurumurthy, Meera, Shengli Xu, Kong Peng Lam, Nge Cheong, and Sheng-Hao Chao

Subjects
*HEXAMETHYLENEBISACETAMIDE, *RNA polymerases, *NUCLEOPHOSMIN, *ACUTE myeloid leukemia, *COLON cancer, *PROTEIN-protein interactions, *ANTINEOPLASTIC agents, *DOXORUBICIN
Abstract

Hexamethylene bisacetamide-inducible protein 1 (HEXIM1) is best known as the inhibit or of positive transcription elongation factor b (P-TEFb), which regulates the transcription elongation of RNA polymerase II and controls 60-70% of mRNA synthesis. Our previous studies show that HEXIM1 interacts with two key p53 regulators, nucleophosmin and human double minute-2 protein (HDM2), implying a possible connection between HEXIM1 and the p53 signaling pathway. Here we report the interaction between p53 and HEXIM1 in breast cancer, acute myeloid leukemia, and colorectal carcinoma cells. The C-terminal regions of p53 and HEXIM1 are required for the protein-protein interaction. Overexpression of HEXIM1 prevents the ubiquitination of p53 byHDM2and enhances the protein stability of p53, resulting in up-regulation of p53 target genes, such as Puma and p21. Induction of p53 can be achieved by several means, such as UV radiation and treatment with anticancer agents (including doxorubicin, etoposide, roscovitine, flavopiridol, and nutlin-3). Under all the conditions examined, elevated protein levels of p53 are found to associate with the increased p53-HEXIM1 interaction. In addition, knockdown of HEXIM1 significantly inhibits the induction of p53 and releases the cell cycle arrest caused by p53. Finally, the transcription of the p53 target genes is regulated by HEXIM1 in a p53-dependent fashion. Our results not only identify HEXIM1 as a positive regulator of p53, but also propose a novel molecular mechanism of p53 activation caused by the anti-cancer drugs and compounds. [ABSTRACT FROM AUTHOR]

Published
2012
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30. Adjunctive pascolizumab in rifampicin-susceptible pulmonary tuberculosis: proof-of-concept, partially-randomised, double-blind, placebo-controlled, dose-escalation trial.

Author

Paton NI, Gurumurthy M, Lu Q, Leek F, Kwan P, Koh HWL, Molton J, Mortera L, Naval S, Abu Bakar Z, Pang YK, Lum L, Lim TK, Cross GB, Lekurwale G, Choi H, Au V, Connolly J, Hibberd M, and Green JA

Abstract

Background: Interleukin-4 (IL-4), increased in tuberculosis infection, may impair bacterial killing. Blocking IL-4 confers benefit in animal models. We evaluated safety and efficacy of pascolizumab (humanised anti-IL-4 monoclonal antibody) as adjunctive tuberculosis treatment., Methods: Participants with rifampicin-susceptible pulmonary tuberculosis received a single intravenous infusion of pascolizumab or placebo; and standard 6-month tuberculosis treatment. Pascolizumab dose increased in successive cohorts: [1] non-randomised 0.05 mg/kg (n = 4); [2] non-randomised 0.5 mg/kg (n = 4); [3] randomised 2.5 mg/kg (n = 9) or placebo (n = 3); [4] randomised 10 mg/kg (n = 9) or placebo (n = 3). Co-primary safety outcome was study-drug-related grade 4 or serious adverse event (G4/SAE); in all cohorts (1-4). Co-primary efficacy outcome was week-8 sputum culture time-to-positivity (TTP); in randomised cohorts (3-4) combined., Results: Pascolizumab levels exceeded IL-4 50% neutralising dose for 8 weeks in 78-100% of participants in cohorts 3-4. There were no study-drug-related G4/SAEs. Median week-8 TTP was 42 days in pascolizumab and placebo groups (p = 0.185). Rate of TTP increase was greater with pascolizumab (difference from placebo 0.011 [95% Bayesian credible interval 0.006 to 0.015] log10TTP/day., Conclusions: There was no evidence to suggest blocking IL-4 was unsafe. Preliminary efficacy findings are consistent with animal models. This supports further investigation of adjunctive anti-IL-4 interventions for tuberculosis in larger phase 2 trials., (© The Author(s) 2024. Published by Oxford University Press on behalf of Infectious Diseases Society of America. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.)

Published
2024
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