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Amit Singh
Assistant Professor
PhD (University of Delhi, South Campus
Phone: +91 8022933063, +91 8022933273, +91 8022933275
E.mail:asingh@mcbl.iisc.ernet.in
Lab Web Page : http://cidr.iisc.ernet.in/amit/

Fundamental mechanisms regulating mycobacterial persistence: Mycobacterium tuberculosis (Mtb) is an extremely successful pathogen due to its ability to persist, and to latently infect more than one third of the world’s population. How Mtb can persist in human tissues for decades without replicating and then abruptly resume growth and cause disease is a fundamental question in the TB field. Understanding the molecular mechanism(s) of Mtb dormancy and reactivation has become the focus of increased attention chiefly because Mtb persists in a drug-tolerant.


Development of basic tools to track physiology of Mtb during infection: Persistence of Mtb in host phagocytes depends on its ability to resist oxidant-mediated antibacterial responses. Mycothiol (MSH) is the main antioxidant that provides an abundant source of reducing equivalent, which protects Mtb from oxidative stress encountered during infection. We have successfully developed a novel and noninvasive tool based on genetically encoded redox sensitive fluorescent probes to perform real-time measurement of mycothiol redox potential (EMSH) in Mtb during infection. For the first time we reveal the EMSH of virulent and avirulent mycobacterial strains, including drug-resistant clinical isolates.


HIV infection and oxidative stress: HIV infected patients suffer from chronic oxidative stress. Our lab aims to develop a series of non-invasive biosensors to measure oxidative changes associated with HIV infection in real-time. This study will provide mechanistic understanding of redox basis of HIV infection and lead to better development of more affordable anti-oxidant based strategies for the control of AIDS.

Selected Publications

Amit Singh, Mai D, Kumar A, and Steyn AJC. Dissecting virulence pathways of Mycobacterium tuberculosis through protein-protein association. Proc Natl Acad Sci USA, 2006, 103,11346-51.

Amit Singh, Guidry L, Narasimhulu K V, Mai D, Trombley J, Redding K E, Giles G I, Lancaster J Jr and Steyn AJC. Mycobacterium tuberculosis WhiB3 responds to O2 and nitric oxide via its [4Fe-4S] cluster and is essential for nutrient starvation survival.  Proc Natl Acad Sci USA, 2007, 104,11562-11567.

Amit Singh, Crossman D K, Mai D, Guidry L, Voskuil M V, Renfrow M B and Steyn AJC. Mycobacterium tuberculosis WhiB3 maintains intrabacterial redox homeostasis by modulating virulence lipid anabolism to subvert innate immunity PLoS Pathog, 20095, e1000545.

Karim, FA., Chandra, P., Chopra, A., Siddiqui, J., Bhaskar, A., Amit Singh, & Kumar D. Express Path Analysis Identifies a Tyrosine Kinase Src-centric Network Regulating Divergent Host Responses to Mycobacterium tuberculosis InfectionJ. Biol. Chem, 2011, 286, 40307-40319.

Chawla M, Parikh P, Saxena A, Munshi M, Mehta M, Mai D, Srivastava AK, Narasimhulu KV, Redding KE, Vashi N, Kumar D, Steyn AJ, & Amit Singh. Mycobacterium tuberculosis WhiB4 regulates oxidative stress response to modulate survival and dissemination in vivo.  Mol Microbiol, 2012, 85,1148-65.

Bhaskar A, Chawla M, Mehta M, Parikh P, Chandra, Kumar D, Bhave D, Carroll K, and Amit Singh. Reengineering redox sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection. PLoS Pathog, 2014, journal.ppat.1003902.