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Significance Secreted bacterial phospholipases, which hydrolyze host membranes, may also harm the pathogen itself. Sophisticated activation mechanisms are therefore required to prevent self-damage before protein export but warrant activity at the pathogen–host interface. Here we structurally analyzed PlaB, a surface-exposed highly active phospholipase and virulence factor of the lung pathogenLegionella pneumophila . Unexpectedly, we found that NAD(H), a central cofactor of energy metabolism, stabilizes an inactive tetrameric form of PlaB. Since NAD(H) is confined to the intracellular milieu of the bacterium, we propose that this sophisticated NAD(H)-dependent oligomerization mechanism protectsL. pneumophila from damage and simultaneously enables the function of PlaB as a virulence factor after export and association to the bacterial surface.

NAD(H)-mediated tetramerization controls the activity of Legionella pneumophila phospholipase PlaB