Abstract 1734 Systematic identification of Legionella's phosphoinositide-binding arsenal unveils distinct folds

Phosphoinositide (PIP) lipids are integral regulators of eukaryotic membrane traffic acting as molecular beacons that recruit and activate protein complexes. The seven different PIP species confer membrane identity as they are each found specifically enriched on distinct cellular membranes. Recently, PIPs have emerged as a target of intracellular bacterial pathogens that exploit host membranes. The intracellular human pathogen, Legionella pneumophila, infects and proliferates within lung macrophages.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109616
Primary Topic
Legionella and Acanthamoeba research
Type
article
Field-Weighted Citation Impact
0.00
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Abstract 1734 Systematic identification of Legionella's phosphoinositide-binding arsenal unveils distinct folds

Ramona Neunuebel, A. Richardson, Sylvain Marchand, Alicia M. Bolt et al.
Journal of Biological Chemistry
Legionella and Acanthamoeba research
article

Abstract 1734 Systematic identification of Legionella's phosphoinositide-binding arsenal unveils distinct folds

Ramona Neunuebel, A. Richardson, Sylvain Marchand, Alicia M. Bolt, Karl R. Schmitz
article en

Abstract

Phosphoinositide (PIP) lipids are integral regulators of eukaryotic membrane traffic acting as molecular beacons that recruit and activate protein complexes. The seven different PIP species confer membrane identity as they are each found specifically enriched on distinct cellular membranes. Recently, PIPs have emerged as a target of intracellular bacterial pathogens that exploit host membranes. The intracellular human pathogen, Legionella pneumophila, infects and proliferates within lung macrophages.

Journal of Biological ChemistryVol. 301(5)
University of Delaware (US)
Zero hunger
Openalex Percentile: Top 89%
Legionella and Acanthamoeba research
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