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The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection
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The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection
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Journal Article
The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection
2015
Overview
The mechanisms that control activation of the AIM2 inflammasome by cytosolic bacteria are unclear. Kanneganti and colleagues demonstrate that a pathway involving the transcription factor IRF1 is required for the activation of AIM2.
Inflammasomes are critical for mounting host defense against pathogens. The molecular mechanisms that control activation of the AIM2 inflammasome in response to different cytosolic pathogens remain unclear. Here we found that the transcription factor IRF1 was required for activation of the AIM2 inflammasome during infection with the
Francisella tularensis
subspecies
novicida
(
F. novicida
), whereas engagement of the AIM2 inflammasome by mouse cytomegalovirus (MCMV) or transfected double-stranded DNA did not require IRF1. Infection of
F. novicida
detected by the DNA sensor cGAS and its adaptor STING induced type I interferon–dependent expression of IRF1, which drove the expression of guanylate-binding proteins (GBPs); this led to intracellular killing of bacteria and DNA release. Our results reveal a specific requirement for IRF1 and GBPs in the liberation of DNA for sensing by AIM2 depending on the pathogen encountered by the cell.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ 13/109
/ 13/21
/ 13/31
/ 13/51
/ 13/89
/ 13/95
/ 14/19
/ 96/31
/ Animals
/ DNA
/ DNA-Binding Proteins - metabolism
/ Francisella tularensis - physiology
/ Gene Expression Regulation - genetics
/ GTP-Binding Proteins - metabolism
/ Interferon Regulatory Factor-1 - genetics
/ Interferon Regulatory Factor-1 - metabolism
/ Interferon Type I - metabolism
/ Mice
