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Legionella pneumophila SidD is a deAMPylase that modifies Rab1

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  • Yunhao Tan

    (Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA)

  • Zhao-Qing Luo

    (Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA)

Abstract

A pathogen's protein armoury Legionella pneumophila secretes multiple effectors into host cells during infection, some of which modify host trafficking and thereby aid intracellular replication. One of these modifications is AMPylation of Rab1 by L. pneumophila SidM. This study adds another layer to this regulation by demonstrating that a second L. pneumophila effector, SidD, deAMPylates Rab1. The identification of SidD suggests that this pathogen uses a specific set of proteins to hijack the activity of Rab1 for its own purposes.

Suggested Citation

  • Yunhao Tan & Zhao-Qing Luo, 2011. "Legionella pneumophila SidD is a deAMPylase that modifies Rab1," Nature, Nature, vol. 475(7357), pages 506-509, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7357:d:10.1038_nature10307
    DOI: 10.1038/nature10307
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    Cited by:

    1. Yizhi Yuan & Florian M. Stumpf & Lisa A. Schlor & Olivia P. Schmidt & Philip Saumer & Luisa B. Huber & Matthias Frese & Eva Höllmüller & Martin Scheffner & Florian Stengel & Kay Diederichs & Andreas M, 2023. "Chemoproteomic discovery of a human RNA ligase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Marietta S. Kaspers & Vivian Pogenberg & Christian Pett & Stefan Ernst & Felix Ecker & Philipp Ochtrop & Michael Groll & Christian Hedberg & Aymelt Itzen, 2023. "Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Tobias Sahr & Pedro Escoll & Christophe Rusniok & Sheryl Bui & Gérard Pehau-Arnaudet & Gregory Lavieu & Carmen Buchrieser, 2022. "Translocated Legionella pneumophila small RNAs mimic eukaryotic microRNAs targeting the host immune response," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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