Nanostructure of the S. pneumoniae division ring

What is it about?

Deciphering bacterial division mechanisms is required for discovering new antibacterial targets. Using a state-of-the art microscopy technique, this work provides insight at the nanoscale into the assembly of a key protein complex along the cell cycle of S. pneumoniae, a major human pathogen.

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Why is it important?

The Gram-positive human pathogen S. pneumoniae is responsible for 1.6 million deaths per year worldwide and is increasingly resistant to various antibiotics. Our work focuses on FtsZ, which is a promising new antimicrobial target, as its inhibition leads to cell death. A precise view of the Z-ring architecture in vivo is essential to understand the mode of action of inhibitory drugs. This is notably true in ovococcoid bacteria like S. pneumoniae, in which FtsZ is the only known cytoskeletal protein. We have used superresolution microscopy to obtain molecular details of the pneumococcus Z-ring that have so far been inaccessible with conventional microscopy. This study provides a nanoscale description of the Z-ring architecture and remodeling during the division of ovococci.