Tracking fluorescent fusion proteins in competent pneumococcal cells reveals a polar hub for competence regulation, with the alternative sigma factor σX relocalizing DprA to this hub to mediate competence shut-off.

A respiratory tissue-associated commensal Lactobacillus strain confers colonization resistance to Streptococcus pneumoniae, when applied therapeutically in a post influenza virus super-infection model.

Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.

DNA uptake and recombination in pneumococcus are highly efficient and independent of the cell-cycle or genetic location of the transformed allele, but limited to maximally 50% of the population.

To avoid recognition by the immune system, bacteria use autolysins to trim fragments of peptidoglycans that are exposed on the bacterial cell wall.

Bacterial-encoded covalent adhesion is a new molecular principle in host-microbe interactions and may play a key role in host colonization by a wide range of Gram-positive bacteria.

The near-atomic cryoEM pore complex structure of pneumolysin, the main virulence factor of Streptococcus pneumoniae, shows how the individual domains rearrange during the pore formation.

Being able to take up DNA from their environment might allow pneumococcal bacteria to colonize the human nose and throat for longer periods of time.

Bacillus subtilis can measure the activity of the enzymes that remodel the cell wall to ensure that the levels of activity are ‘just right’.