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

A novel component of type III protein secretion systems involved in the assembly of the secretion machine is reported.

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.

Biochemical analyses and the crystal structure of TtsA reveal fundamental insight into the mechanisms by which this muramidase recognizes its peptidoglycan substrate to facilitate typhoid toxin secretion.

Visualization of the type III secretion mediated Salmonella-host cell interface reveals the intact translocon and the profound remodeling of the host membrane at unprecedented resolution.

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

Communities of bacteria that cause Legionnaire’s disease repel other bacteria by secreting an acid called HGA.

The induction of ISG15 during bacterial infection can be independent of Type I Interferons and leads to an increase in the secretion of cytokines known to be critical for bacterial clearance.

The basal body of the type-III secretion system of Yersinia enterocolitica within bacterial membranes shows elasticity and is longer than related isolated systems.