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

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

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

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

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 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.

Current models of Alzheimer's disease that put mitochondria as an endpoint of disease should be reconsidered because genetic defects affecting mitochondria by themselves can also regulate Alzheimer’s disease risk factor apolipoprotein E (APOE) expression and secretion.

Genetic, biochemical, and cell biological approaches reveal a new form of contact-dependent inhibition in bacteria involving bacteriocin-like proteins that aggregate on the surface of cells.

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

Using both electron cryo-tomography and helical reconstruction, the first structure of the entire archaellum machinery with an assembled filament has been determined, providing the structural basis for our understanding of archaeal motility.