Mémoire
| Résumé : | Bacterial toxin-antitoxin (TA) systems generally consist of a two-gene operon encoding a toxin, which disrupts cellular homeostasis, and a toxin-inhibiting antitoxin. In some cases, SecB-like chaperones associate with TA systems, forming tripartite toxin-antitoxin-chaperone (TAC) modules. While TACs are known to protect against bacteriophage infections, the processes by which they detect and inhibit viruses remain unclear. This study examines how the SecB-like chaperone HigC, associated with the host-inhibition of growth (Hig) HigBAC TAC system in Escherichia coli, detects the lambda (λ) phage major tail tube protein gpV and initiates an abortive infection mechanism to protect the bacterial population from phage propagation. These findings provide novel insights into the dynamic interplay between viral infection and bacterial immunity, advancing our understanding of microbial defence mechanisms and potentially informing the development of new antibacterial strategies. |
