Legionella pneumophila can be inhibited by its own antimicrobial, HGA (homogentisic acid), but its density-dependent resistance to HGA restricts the potential for self-harm.

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

A correlation between the periplasmic embellishment of the flagellar motor and its stator system type is described, motors with dual H+-dependent stator systems have one periplasmic ring formed by MotY.

Legionella effector RavZ evades host autophagy by extracting LC3-PE from the membrane before deconjugation.

Infected cells superinduce expression of mRNA in order to initiate an immune response to a bacterial pathogen that blocks host protein synthesis.

The pseudokinase-like Legionella effector SidJ catalyzes the glutamylation of bacterial ubiquitin ligases in a calmodulin-dependent manner.

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

A novel class of bacterial OTU deubiquitinases provides insights on the distinct roles of bacterial deubiquitinases in host–pathogen interactions.

Structural and biochemical studies reveal the molecular mechanisms for ubiquitin transfer by two unique bacterial ubiquitin E3 ligases.

Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.