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- W2000945611 abstract "Upon infection of many bacterial pathogens, bacterial invasion is quickly sensed by the innate immune system, resulting in acute inflammatory responses. However, it is still unclear how pathogens modulate host inflammatory responses to bacterial internalization into epithelial cells. Here we provide evidence that the Shigella flexneri effector OspI delivered via the type III secretion system dampens acute inflammatory responses during bacterial invasion of epithelial cells by targeting TNF receptor-associated factor 6 (TRAF6). We found that OspI can bind to UBC13, an E2 ubiquitin-conjugating enzyme, and act as a unique glutamine deamidase by selectively deamidating Gln100 to Glu100 in UBC13. Consequently, the E2 ubiquitin-conjugating activity that is required for TRAF6 activation was inhibited, allowing S. flexneri OspI to modulate the diacylglycerol-CBM complex-TRAF6-NFκB signaling pathway. We determined the 2.0 A crystal structure of OspI, which contains a putative Cys-His-Asp catalytic triad. A mutational analysis showed that this catalytic triad was essential for the deamidation activity. Our results highlight a unique bacterial tactic that modulates acute inflammatory responses to bacterial invasion of epithelial cells by targeting the UBC13-TRAF6 complex." @default.
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- W2000945611 date "2012-10-01" @default.
- W2000945611 modified "2023-10-05" @default.
- W2000945611 title "A bacterial effector targets the TRAF6-NFκB pathway to modulate the acute inflammatory response to bacterial invasion of epithelial cells" @default.
- W2000945611 doi "https://doi.org/10.4161/viru.21451" @default.
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