Legionella Metaeffector Exploits Host Proteasome to Temporally Regulate Cognate Effector

PLoS Pathogens

Naoaki Shinzawa¹  Hirotaka Kanuka²  Hiroki Nagai²  Tomoko Kubori³ 

[1] Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan;National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, Japan;Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan

关键词: Legionella pneumophila;    Host cells;    Ligases;    Legionella;    Ubiquitin ligases;    Bacterial pathogens;    Proteasomes;    Glutathione chromatography;   

DOI  :  10.1371/journal.ppat.1001216

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Pathogen-associated secretion systems translocate numerous effector proteins into eukaryotic host cells to coordinate cellular processes important for infection. Spatiotemporal regulation is therefore important for modulating distinct activities of effectors at different stages of infection. Here we provide the first evidence of “metaeffector,” a designation for an effector protein that regulates the function of another effector within the host cell. Legionella LubX protein functions as an E3 ubiquitin ligase that hijacks the host proteasome to specifically target the bacterial effector protein SidH for degradation. Delayed delivery of LubX to the host cytoplasm leads to the shutdown of SidH within the host cells at later stages of infection. This demonstrates a sophisticated level of coevolution between eukaryotic cells and L. pneumophila involving an effector that functions as a key regulator to temporally coordinate the function of a cognate effector protein.

【 授权许可】

CC BY