Special Scientific Lecture on Investigate phage-bacteria interactions to explore novel bacterial immune systems and phage-derived antimicrobials



03 - June -2024    Duration: 11:00 AM To 12:00 PM

Venue: CSIR-IMTECH

All are cordially invited to a special scientific lecture by Dr. Tridib Mahata on 3rd June 2024 at 11:00 AM in the seminar hall, main building. Currently, Dr. Tridib Mahata is working as a Postdoc fellow in the Department of Clinical Microbiology and Immunology, School of Medicine, Tel Aviv University, Israel. He obtained his PhD from CSIR-IICT, Hyderabad.



Title: Investigate phage-bacteria interactions to explore novel bacterial immune systems and phage-derived antimicrobials

Date and Time: 3rd June 2024 at 11 AM

Venue: Seminar Hall, Main Building, CSIR-IMTech

 

Abstract of the talk:

Bacteriophages and bacteria engage in a constant arms race, developing defense and anti-defense systems. Bacteriophages have evolved multiple strategies to target host metabolic pathways, while bacteria have developed various defense mechanisms against phage predation. Our research has identified specific phage-encoded gene products, T5.008 and T5.015, which inhibit bacterial cell growth by targeting key components of E. coli. T5.008 disrupts the FtsZ ring, inhibiting cell division and granting T5 a selective advantage (1). T5.015 binds with Uracil DNA glycosylase (Ung) to selectively nick dUMP-containing DNA, leading to replication blockage and cell division inhibition (2). These unique mechanisms make T5.008 and T5.015 potential antimicrobial agents. Furthermore, we've discovered a widespread genetic element characterized by the presence of Gamma-Mobile-Trio (GMT) proteins, functioning as a mobile bacterial weapons arsenal. GMT islands are active mobile elements, containing secreted antibacterial toxins and anti-phage defense systems. This discovery has allowed us to identify four new anti-phage defense systems encoded within GMT islands, including a novel immune system with a nuclease domain that induces cell dormancy upon activation by a phage capsid protein (3).