Room No. 509, 5th Floor,
Host-pathogen interactions and cell signalling Lab,
Molecular Cell Biology.
We are investigating the interactions of some of the proteins of M. tuberculosis which are responsible for enhanced intracellular survival and virulence. PTMs of M. tuberculosis proteins within host are also being examined. We have also initiated the project on the screening of small molecules with an aim to unravel new class of antibiotics which may inhibit the interactions of Mtb proteins with host proteins, thus affecting the intracellular survival of Mtb. Recently, we have initiated the studies to identify novel mutations in clinical isolates conferring resistance to second line drugs of Tuberculosis.
Ganaie, A. A.*, Trivedi, G*., Kaur, A*., Jha, S. S., Anand, S., Rana, V., Singh, A., Kumar, S and Sharma, C. (2016) Increase in adenylate cyclase activity of Rv2212 upon interaction with Erp protein of Mtb enhances Mycobacterium survival within macrophages. J. Bact. 198(20):2841-2852.
Kaur, S*., Rana, V*., Singh, P., Trivedi, G., Anand, S., Kaur, A., Gupta, P., Jain A. and Sharma C. (2016) Novel mutations conferring resistance to kanamycin in Mycobacterium tuberculosis clinical isolates from Northern India. Tuberculosis 96:96-101.
Ganaie, A. A*., Lella, R. K*., Solanki, R. and Sharma, C. (2011) Hexameric form of Eis (Rv 2416c) Protein of Mycobacterium tuberculosis is Responsible for Thermostable Aminoglycoside Acetyltransferase Activity. PLoS ONE 6(11):e27590.
Lella, R. K., and Sharma, C. (2007) Eis (Enhanced Intracellular Survival) protein of Mycobacterium tuberculosis disturbs the cross regulation of T-cells. J. Biol. Chem. 282(26): 18671-18675.
Meher, A., Lella, R. K., Sharma, C. and Arora, A. (2007) Analysis of complex formation and immune response of CFP-10 and ESAT-6 complex. Vaccine 25(32):6098-6106.