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