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.

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.

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.

Panproteome array analysis of antibody responses to a pneumococcal whole cell vaccine reveals consistent induction of immune responses to multiple surface proteins, despite individuals' unique pre-existing antibody profiles.

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.

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.

Sequence changes in the pneumococcal genome explain most of the variability in duration of asymptomatic carriage with serotype, antibiotic resistance and prophage accounting for the largest effects.

Penicillin induces bacterial cell lysis by altering cell surface polymer biogenesis to cause the misactivation of a cell wall degrading enzyme.