Antibacterial potency of type VI amidase effector toxins is dependent on substrate topology and cellular context.

ABSTRACT: Members of the bacterial T6SS amidase effector (Tae) superfamily of toxins are delivered between competing bacteria to degrade cell wall peptidoglycan. Although Taes share a common substrate, they exhibit distinct antimicrobial potency across different competitor species. To investigate the molecular basis governing these differences, we quantitatively defined the functional determinants of Tae1 from Pseudomonas aeruginosa PAO1 using a combination of nuclear magnetic resonance and a high-throughput in vivo genetic approach called deep mutational scanning (DMS). As expected, combined analyses confirmed the role of critical residues near the Tae1 catalytic center. Unexpectedly, DMS revealed substantial contributions to enzymatic activity from a much larger, ring-l

SUBMITTER: Radkov A 

PROVIDER: S-EPMC9270033 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature