Membrane-dependent actin polymerization mediated by the Legionella pneumophila effector protein MavH.

ABSTRACT: L. pneumophila propagates in eukaryotic cells within a specialized niche, the Legionella -containing vacuole (LCV). The infection process is controlled by over 330 effector proteins delivered through the type IV secretion system. In this study, we report that the Legionella MavH effector harbors a lipid-binding domain that specifically recognizes PI(3)P (phosphatidylinositol 3-phosphate) and localizes to endosomes when ectopically expressed. We show that MavH recruits host actin capping proteins (CP) and actin to the endosome via its CP interacting (CPI) motif and WH2-like actin-binding domain, respectively. In vitro assays revealed that MavH stimulates robust actin polymerization only in the presence of PI(3)P-containing liposomes and the recruitment of CP by MavH neg

SUBMITTER: Zhang Q 

PROVIDER: S-EPMC9900769 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature