Urmi Bajpai
Acharya Narendra Dev College, University of Delhi
Professor Urmi Bajpai, from the Department of Biomedical Science at Acharya Narendra Dev College, University of Delhi, focuses on developing antibacterial strategies using endolysins and small molecule inhibitors for multi-target therapy against Mycobacterium tuberculosis. Her work contributes to multi-centric projects on antimicrobial resistance, One Health, and bacteriophages. She is a co-founder of the International Bacteriophage Research Consortium (IBRC) and serves as Vice President of the Society of Bacteriophage Research and Therapy in India. Professor Bajpai has received several national awards in recognition of her contributions to education and research.
Affiliations: (1). Acharya Narendra Dev College, University of Delhi (India) (2). National Jalma Institute of Leprosy & Other Mycobacterial Diseases (India)
Tuberculosis (TB) is a curable infectious disease. However, the lengthy treatment regimen and drug toxicity, and the multidrug-resistant infections, pose significant challenges to TB patients, causing extensive suffering and disability compounded by economic hardships. The incidence of drug-resistant non-tuberculous mycobacterial (NTM) infections is also increasing globally. Hence, there is an urgent need to discover alternative antimycobacterial solutions. Endolysins, with their rapid and precise action against planktonic cells and biofilms, can be promising adjuncts to TB drugs and potentially reduce drug dosage and associated toxicity. We have a repertoire of mycobacteriophage-encoded endolysins (LysinA & LysinB), demonstrating varied domain architecture. In my talk, I will share data on the endolysins we have purified as recombinant proteins and functionally characterized using biochemical and antibacterial assays such as plate lysis, log-kill and biofilm-inhibition assays. Some endolysins possess intrinsic antibacterial properties and induced cell lysis upon external application, an essential trait for natural lysins to act as antibiotics. Also, will present biochemical and antibacterial profiling of a LysinB that shows significantly high esterase activity (5.1 U/mg), indicating catalytic efficiency, inhibits M. smegmatis biofilm formation by >75% and exhibits lytic activity against H37Rv and MDR strains of M. tuberculosis and M. fortuitum, making it a promising antimycobacterial candidate.