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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.

MakA, a pore-forming cytotoxin produced by Vibrio cholerae, forms oligomers and remodels membranes into high-curvature tubes, resulting in membrane integrity loss inside acidified organelle lumens or when cultured with cells in an acidic medium.

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.

A phage parasite encodes an external scaffolding protein to pirate and rearrange phage-encoded coat proteins to more efficiently transfer the phage parasite genome to new hosts and limit phage production.

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

RNA degradation is completed through specific intermediates, such as diribonucleotides, which must be removed from the cells by a specific enzyme.

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

The growth of multicellular bacterial structures called biofilms generates forces that deform soft material substrates and disrupt epithelial cell layers, potentially mechanically damaging host tissue.

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

Horizontal transfer of a sequence-specific DNA-binding domain allows a virus to destroy its subviral parasite and overcome parasite-mediated restriction.