A quorum-sensing-controlled program of multicellularity, aggregation, is identified in Vibrio cholerae, which may be important for transitions between the marine niche and the human host.

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

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.

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.