The structure of the endogenous ESX-3 secretion system reveals a highly coordinated inner membrane complex and suggests a mechanism for the regulated secretion of ESX substrates.

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

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

A widespread family of chaperones functions to stabilize membrane protein effectors by mimicking transmembrane helical environments and promotes effector export by the bacterial type VI secretion system.

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

Microbial genetics and biophysical analyses provide insight into an evolutionarily conserved bile salt receptor complex used by pathogenic bacteria to sense their environment.

Genetic code expansion (GCE) enables site-specific labeling and visualization of Salmonella secreted effectors, secretion system components and provides a viable alternative for labeling proteins that do not tolerate N- or C-terminal tags.

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

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

AatD is a novel acyltransferase that mediates N-palmitoylation of glycine, a process not previously described, that results in the secretion of lipoproteins to the bacterial cell surface.