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.

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

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.

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

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

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

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.

Human macrophages infected with Mycobacterium tuberculosis present peptides derived from substrates of type VII secretion systems on MHC class I via a pathway dependent on the ESX-1 secretion system and independent of antigen processing by the proteasome and cathepsins.

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