The enterococcal adhesin PrgB consists of four immunoglobulin-like domains that support the proper function of its polymer adhesin domain.

Salmonella antibacterial effectors act on Y-shaped DNA substrates resembling replication forks or transcription bubbles and lead to DNA double-strand breaks.

During infection, L. pneumophila reverses the ATP-synthase activity of the mitochondrial F_OF₁-ATPase to ATP-hydrolase activity in a type 4 secretion-dependent manner to prevent early cell death, thereby preserving its replication niche.

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.

A multidisciplinary approach provides a description of the exocytic pathway that exports Salmonella Typhi's typhoid toxin from infected cells.

Considering the course of a pathogen's evolution, there appears to be interplay between secretion systems, providing unique, synergistic mechanisms to support a successful lifestyle for possibly pathogenesis, symbiosis and/or parasitosis.

SatS of Mycobacterium tuberculosis is a new protein export chaperone with a role in exporting proteins by the specialized SecA2 pathway and a role in intracellular growth in macrophages.

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.

Genes for adhesion, interbacterial competition, and secondary metabolite production are important colonization factors of the honey bee gut symbiont Frischella perrara and are regulated by the conserved histone-like DNA-binding protein integration host factor.

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.