Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

The Helicobacter pylori Cag T4SS has unique structural features, including unexpected symmetry mismatch between sub-complexes, with implications for protein secretion.

The structure of a Type IV secretion system provides a framework for understanding assembly of a protein-injection machine.

The structure of the Legionella pneumophilaType IV secretion system provides the detailed molecular model of this complex molecular machine required for pathogenesis.

Structural analysis of the type IV secretion system purified from Legionella pneumophila uncovers new complex components and symmetry mismatches.

The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.

A novel bacterial deubiquitinase with multiple chain types specificity regulates the association of ubiquitinated proteins on the phagosome of Legionella pneumophila.

The upper airway commensal, Neisseria cinerea, competes with related species using a T6SS, with antagonism modulated by the spatial dynamics of attacker and prey strains growing in a mixed community.

Sera from vaccinated subjects bound additional linear epitopes compared to sera from individuals with mild infection, in addition the pathways of escape from antibodies from vaccination were more uniform than those from mildly infected individuals.

Legionella pneumophila modulates host energy metabolism by targeting the ADP/ATP translocase carrier proteins with an effector of ADP-ribosyltransferase activity.