The versatile Legionella effector protein DrrA

The human pathogen Legionella pneumophila is a bacterium that infects human cells and interferes with intracellular signaling. The Legionella protein DrrA is one of the numerous effectors that the bacterium translocates into the host cytosol. DrrA binds to the Legionella containing vacuole (LCV), an...

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Bibliographic Details
Published inCommunicative & integrative biology Vol. 4; no. 1; pp. 72 - 74
Main Authors Goody, Roger S., Müller, Matthias P., Schoebel, Stefan, Oesterlin, Lena K., Blümer, Julia, Peters, Heide, Blankenfeldt, Wulf, Itzen, Aymelt
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 01.01.2011
Subjects
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cycle
Landes
Organogenesis
Proteins
Rab
Legionella containing vacuole
adenylylation
GEF
Legionella
vesicular trafficking
phosphoinositide
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Summary:The human pathogen Legionella pneumophila is a bacterium that infects human cells and interferes with intracellular signaling. The Legionella protein DrrA is one of the numerous effectors that the bacterium translocates into the host cytosol. DrrA binds to the Legionella containing vacuole (LCV), an organelle in which Legionella survives and replicates, and recruits and activates the vesicular trafficking regulator Rab1 to redirect vesicular trafficking between the endoplasmatic reticulum and the Golgi. After depositing Rab1 at the LCV, DrrA covalently modifies Rab1 with an AMP moiety at a specific tyrosine residue (Tyr77), which is centrally located in the functionally important switch II region. This adenylylation reaction interferes with the deactivation of Rab1 by GTPase activating proteins (GAPs), thereby presumably prolonging the active state of the protein at the LCV. Here, we summarize the versatile properties of DrrA and speculate on the effects of Rab1-adenylylation.
ISSN:1942-0889
1942-0889
DOI:10.4161/cib.13857