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Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer.
A Cre/loxP-based protein translocation assay is found that proteins translocated by the Dot/Icm complex across the host phagosomal membrane can also be transferred from one bacterial cell to another.
Ubiquitination independent of E1 and E2 enzymes by bacterial effectors
It is established that ubiquitination can be catalysed by a single enzyme, the activity of which does not require ATP.
Secreted Bacterial Effectors That Inhibit Host Protein Synthesis Are Critical for Induction of the Innate Immune Response to Virulent Legionella pneumophila
These results provide a striking illustration of how the host immune response to a virulent pathogen can also be shaped by pathogen-encoded activities, such as inhibition of host protein synthesis.
Quorum‐sensing signal binding results in dimerization of TraR and its release from membranes into the cytoplasm
It is concluded that binding signal drives dimerization of TraR and its release from membranes into the cytoplasm and the N‐terminus from cells grown without signal is hidden.
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
It is found that the deAMPylation activity of SidD could suppress the toxicity of SidM to yeast and is required to release Rab1 from bacterial phagosomes efficiently to indicate that AMPylation-mediated signal transduction is a reversible process regulated by specific enzymes.
Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response
This work demonstrates that a protein, called SidI, is a substrate of the Dot/Icm type IV protein transporter that targets the host protein translation process and indicates that inhibition of host protein synthesis by specific effectors contributes to the induction of stress response in L. pneumophila‐infected cells.
Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination
Reversible phosphorylcholination is revealed as a mechanism for balanced modulation of host cellular processes by a bacterial pathogen.
Inhibition of Host Vacuolar H+-ATPase Activity by a Legionella pneumophila Effector
This report describes the identification and characterization of a Legionella protein termed SidK that specifically targets host v-ATPase, the multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells, and shows that a domain located in the N-terminal portion of SidK is responsible for its interactions with VatA.
The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling
  • F. Hsu, Xi Luo, +5 authors Y. Mao
  • Biology, Medicine
    Proceedings of the National Academy of Sciences
  • 8 July 2014
Significance Legionella pneumophila, the Legionnaires’ disease-causing bacterial pathogen, translocates a myriad of bacterial proteins, called effectors, into host cells. These proteins exploit
Members of a Legionella pneumophila Family of Proteins with ExoU (Phospholipase A) Active Sites Are Translocated to Target Cells
Detergent extraction studies of infected macrophages confirm that VipD is translocated into host cells via the type IV secretion system, and this protein and its paralogs define a family of translocated proteins that may assist in the establishment of a vacuole suitable for bacterial replication through functioning as a phospholipase.