A single chlamydial protein reshapes the plasma membrane and serves as recruiting platform for central endocytic effector proteins.

ABSTRACT: Uptake of obligate intracellular bacterial pathogens into mammalian epithelial cells is critically dependent on modulation of the host's endocytic machinery. It is an open question how the invading pathogens generate a membrane-bound vesicle appropriate to their size. This requires extensive deformation of the host plasma membrane itself by pathogen-derived membrane-binding proteins, accompanied by substantial F-actin-based forces to further expand and finally pinch off the vesicle. Here we show that upon adhesion to the host cell, the human pathogenic bacterium Chlamydia pneumoniae secretes the scaffolding effector protein CPn0677, which binds to the inner leaflet of the invaginating host's PM, induces inwardly directed, negative membrane curvature, and forms a recruiting platform for the

SUBMITTER: Spona D 

PROVIDER: S-EPMC10182996 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature