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Many bacterial pathogens exploit secretion systems to convey virulence proteins, called effectors, into eukaryotic host cells. Often, these effector proteins are collectively necessary for the progression of infection. The molecular mechanisms by which these effectors support virulence have been the subject of much research. Recent papers analyzing the intracellular fate of Legionella pneumophila effectors have underlined the importance of their subcellular localization in challenging host cellular processes and underscored the exploitation of the eukaryotic lipidation machinery by bacterial pathogens.  The proper localization of proteins to specific subcellular compartments is crucial in the functioning of eukaryotic cells. This is also true and even more critical for prokaryotic proteins given that bacterial effectors are translocated into eukaryotic cells in small quantities. Thus, they need to be directed to their downstream target in order to be able to accomplish their functions.  Similar to eukaryotic proteins synthesized by free ribosomes, translocated effector proteins need to be transported to their intended host compartments and membranes. These include the nucleus (Zurawski et al., 2006), endoplasmic reticulum (Campodonico et al., 2005), plasma membrane (Schmid et al., 2006), or Golgi (Geddes et al., 2005) even though effectors are frequently found in close proximity to their translocation site (Kenny et al., 1997). Targeting of effectors to the cytoplasmic face of endo-membranes is possible owing the presence of hydrophobic domains (Salcedo and Holden, 2003) or the post-translocation modifications by covalent attachment of lipid groups. These modifications facilitate membrane attachment of effectors, their subcellular targeting, and very likely their partitioning into specific membrane domains.

Is Host Lipidation of Pathogen Effector Proteins a General Virulence Mechanism?