Systematic Discovery of Novel Phosphoinositide-Binding Effectors in <i>Legionella</i> Reveals Conserved α-Helical Folds.

ABSTRACT: Intracellular bacterial pathogens deploy effector proteins to hijack host membranes by targeting specific lipids. Phosphoinositides are key eukaryotic signaling molecules that govern membrane identity and dynamics, making them powerful levers for microbial interference. However, the bacterial repertoire of phosphoinositide-binding effectors remains largely undefined. In this study, we systematically identified such proteins using an expression library of 241 Legionella pneumophila effectors. We applied a combination of lipid bead pulldowns, mass spectrometry, colocalization with phosphoinositide biosensors, and protein-lipid overlay assays, leading to the validation of 18 new phosphoinositide-binding effectors. Structural predictions revealed that these proteins share compact alpha-

SUBMITTER: Bolt AE 

PROVIDER: S-EPMC12676380 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature