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Shigella induces stress granule formation by ADP-riboxanation of the eIF3 complex

ABSTRACT: We utilized a large-scale proteomic profiling strategy to quantitatively measure ADP-riboxanation (and classical ADP-ribosylation) levels of host proteins upon introduction of bacterial effectors. Notably, we identified the eukaryotic translation initiation factor 3 (eIF3) complex as a novel target of the OspC family proteins. ADP-riboxanation of eIF3 resulted in inhibition of bulk protein synthesis and SG assembly in infected host cells, which promoted intracellular bacterial proliferation.

ORGANISM(S): Homo Sapiens

SUBMITTER: Xiaoyun Liu

PROVIDER: PXD048666 | iProX | Thu Jan 18 00:00:00 GMT 2024

REPOSITORIES: iProX

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Shigella induces stress granule formation by ADP-riboxanation of the eIF3 complex.

Zhang Qinxin Q Xian Wei W Li Zilin Z Lu Qian Q Chen Xindi X Ge Jinli J Tang Zhiheng Z Liu Bohao B Chen Zhe Z Gao Xiang X Hottiger Michael O MO Zhang Peipei P Qiu Jiazhang J Shao Feng F Liu Xiaoyun X

Cell reports 20240217 2

Under stress conditions, translationally stalled mRNA and associated proteins undergo liquid-liquid phase separation and condense into cytoplasmic foci called stress granules (SGs). Many viruses hijack SGs for their pathogenesis; however, whether pathogenic bacteria also exploit this pathway remains unknown. Here, we report that members of the OspC family of Shigella flexneri induce SG formation in infected cells. Mechanistically, the OspC effectors target multiple subunits of the host translati ...[more]

PMID: 38368608

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