Biofilm matrix protein RbmA controls biofilm architecture through binary structural switching and exopolysaccharide binding.

A structural switch controls the architecture of Vibrio cholerae biofilms by mediating the interactions between two matrix components.

Bacterial viruses are an unexpected ‘third party’ that imposes a strong predatory pressure on a bacterial pathogen during the natural course of infection in humans.

Bacterial cytoplasmic chemoreceptors assemble into a sandwich of two hexagonally packed arrays.

Both beneficial and pathogenic bacteria can use their sheathed flagella during host colonization as a novel toxin-/signal-delivery mechanism.

Studies of the substrate selectivity of concentrative nucleoside transporters provide proof of principle for structure-based improvement of drug delivery by these transporters.

Formation and cell pole-localization of chemotactic signaling-arrays is a coupled process mediated by ParP, which drives localized array-assembly and regulates the localization-dynamics of its network constituents.