Phosphoribosyl ubiquitination of SNARE proteins regulates autophagy during Legionella infection

ABSTRACT: Legionella pneumophila is an intracellular pathogen that causes Legionnaires' disease. The bacteria release effector proteins, some of which remodel host autophagic-lysosomal pathways. One such effector is RavZ, which delipidates ATG8 proteins, making compromising autophagy in Legionella-infected cells. Here we show that SidE effectors also affect these pathways, by mediating phosphoribosyl-ubiquitination (PR-Ub) of the autophagic SNARE proteins STX17 and SNAP29. STX17 modification induces recruitment of STX17-positive membranes from the endoplasmic reticulum to Legionella-containing phagosomes,forming replicative vacuoles. Using proximity labeling, biochemistry and Legionella-infection studies, we define a mechanism by which autophagy is hijacked by bacteria to recruit ER membranes to the

SUBMITTER: Rukmini Mukherjee 

PROVIDER: S-SCDT-10_1038-S44318-025-00483-4 | biostudies-other |

REPOSITORIES: biostudies-other