期刊
CELLULAR MICROBIOLOGY
卷 12, 期 9, 页码 1272-1291出版社
WILEY
DOI: 10.1111/j.1462-5822.2010.01467.x
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资金
- Institut Pasteur
- Centre National de la Recherche (CNRS)
- Network of Excellence 'Europathogenomics' [LSHB-CT-2005-512061]
- Australian National Health and Medical Research Council (NHMRC)
- European Commission [MEST-CT-2005-020715]
- Fondation pour la Recherche Medicale (FRM)
- ANR-ERA-Net
- DIM maladies Infectieuse, Ile de France
P>The environmental pathogen Legionella pneumophila encodes three proteins containing F-box domains and additional protein-protein interaction domains, reminiscent of eukaryotic SCF ubiquitin-protein ligases. Here we show that the F-box proteins of L. pneumophila strain Paris are Dot/Icm effectors involved in the accumulation of ubiquitinated proteins associated with the Legionella-containing vacuole. Single, double and triple mutants of the F-box protein encoding genes were impaired in infection of Acanthamoeba castellanii, THP-1 macrophages and human lung epithelial cells. Lpp2082/AnkB was essential for infection of the lungs of A/J mice in vivo , and bound Skp1, the interaction partner of the SCF complex in mammalian cells, similar to AnkB from strain AA100/130b. Using a yeast two-hybrid screen and co-immunoprecipitation analysis we identified ParvB a protein present in focal adhesions and in lamellipodia, as a target. Immunofluorescence analysis confirmed that ectopically expressed Lpp2082/AnkB colocalized with ParvB at the periphery of lamellipodia. Unexpectedly, ubiquitination tests revealed that Lpp2082/AnkB diminishes endogenous ubiquitination of ParvB. Based on these results we propose that L. pneumophila modulates ubiquitination of ParvB by competing with eukaryotic E3 ligases for the specific protein-protein interaction site of ParvB, thereby revealing a new mechanism by which L. pneumophila may employ translocated effector proteins to promote bacterial survival.
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