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.

Intracellular growth of the bacterial pathogen Legionella pneumophila in the amoeba Dictyostelium discoideum implicates a bacterial fatty acid transporter as well as dynamic interactions of the distinct membrane-bound replication compartment with host cell lipid droplets.

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

A randomized CRISPR-based gene silencing approach overcomes functional redundancy and discovers virulence-critical gene combinations in the pathogen Legionella pneumophila.

Interplay between multiple Legionella pneumophila effector proteins lead to spatial and temporal regulation of the host Rab10 localization to the bacterial vacuole by controlling noncanonical ubiquitin modifications.

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

A novel bacterial protease activated by a eukaryote-specific factor attacks a host protein involved in cytoskeleton organization to inhibit cell migration during Legionella pneumophila infection.

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.

Legionella pneumophila modulates host energy metabolism by targeting the ADP/ATP translocase carrier proteins with an effector of ADP-ribosyltransferase activity.

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.