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

Kevin Bärlocher, Cedric A. J. Hutter, A. Leoni Swart, Bernhard Steiner, Amanda Welin, Michael Hohl, François Letourneur, Markus A. Seeger () and Hubert Hilbi ()
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Kevin Bärlocher: Institute of Medical Microbiology, University of Zürich
Cedric A. J. Hutter: Institute of Medical Microbiology, University of Zürich
A. Leoni Swart: Institute of Medical Microbiology, University of Zürich
Bernhard Steiner: Institute of Medical Microbiology, University of Zürich
Amanda Welin: Institute of Medical Microbiology, University of Zürich
Michael Hohl: Institute of Medical Microbiology, University of Zürich
François Letourneur: UMR5235, DIMNP, CNRS/Université Montpellier
Markus A. Seeger: Institute of Medical Microbiology, University of Zürich
Hubert Hilbi: Institute of Medical Microbiology, University of Zürich

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract 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 (RidL2–281) adopts a “foot-like” fold comprising a protruding β-hairpin at its “heel”. The deletion of the β-hairpin, the exchange to Glu of Ile170 in the β-hairpin, or Leu152 in Vps29 abolishes the interaction in eukaryotic cells and in vitro. RidL2–281 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.

Date: 2017
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DOI: 10.1038/s41467-017-01512-5

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