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Updated: Jun 11, 2026

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
Published on: July 27, 2017
High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA
Stefan Schoebel1, Wulf Blankenfeldt, Roger S Goody
1Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, North Rhine-Westphalia, Germany.
Abstract:
The DrrA protein of Legionella pneumophila is involved in mistargeting of endoplasmic reticulum-derived vesicles to Legionella-containing vacuoles through recruitment of the small GTPase Rab1. To this effect, DrrA binds specifically to phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection. In this study, we present the atomic structure of the PtdIns(4)P-binding domain of a protein (DrrA) from a human pathogen. A detailed kinetic investigation of its interaction with PtdIns(4)P reveals that DrrA binds to this phospholipid with, as yet unprecedented, high affinity, suggesting that DrrA can sense a very low abundance of the lipid.
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