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Legionella pneumophila  can cause Legionnaires’ disease and replicates intracellularly in a distinct  Legionella -containing vacuole (LCV). LCV formation is a complex process that involves a plethora of type IV-secreted effector proteins. The effector RidL binds the Vps29 retromer subunit, blocks retrograde vesicle trafficking, and promotes intracellular bacterial replication. Here, we reveal that the 29-kDa N-terminal domain of RidL (RidL 2–281 ) adopts a “foot-like” fold comprising a protruding β-hairpin at its “heel”. The deletion of the β-hairpin, the exchange to Glu of Ile 170  in the β-hairpin, or Leu 152  in Vps29 abolishes the interaction in eukaryotic cells and in vitro. RidL 2–281  or RidL displace the Rab7 GTPase-activating protein (GAP) TBC1D5 from the retromer and LCVs, respectively, and TBC1D5 promotes the intracellular growth of  L. pneumophila . Thus, the hydrophobic β-hairpin of RidL is critical for binding of the  L. pneumophila  effector to the Vps29 retromer subunit and displacement of the regulator TBC1D5.

Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5