Cholera intoxication of human colonic epithelial cells is dependent on recognition of protein glycosylation and fucosylation, not exclusively on ganglioside recognition as proposed previously.

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.

Structure of the triheteromeric α1β1γ2S GABAA receptor in complex with GABA illuminates the principles of receptor assembly and agonist binding.

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.