![]() ROS regulation of signal transduction allows cellular pathways to rapidly adapt to changes in the oxidative environment.Įven though some pathogens are effectively controlled by ROS, other pathogens thrive in a cellular environment where ROS are abundant ( Paiva and Bozza, 2014). However, accumulating evidence suggests that ROS also control cellular signaling pathways. Due to their capacity to inactivate DNA, proteins and lipids, ROS induce cell death and defend cells against many pathogens. Reactive oxygen species (ROS) are reactive chemicals generated primarily in mitochondria as a byproduct of oxidative metabolism ( Schieber and Chandel, 2014). Together, our findings reveal that ROS orchestrates anti-viral immune responses, which can be exploited by viruses to evade cellular defenses. These data indicate that redox regulation of Cysteine 147 of mouse STING, which is equivalent to Cysteine 148 of human STING, controls interferon production. This inhibited STING polymerization and activation of downstream signaling events. We further demonstrated that ROS suppressed the type I interferon response by oxidizing Cysteine 147 on murine stimulator of interferon genes (STING), an ER-associated protein that mediates interferon response after cytoplasmic DNA sensing. Here, we found that ROS impaired interferon response during murine herpesvirus infection and that the inhibition occurred downstream of cytoplasmic DNA sensing. However, the underlying mechanisms remain unclear. Curiously, some viruses, including herpesviruses, thrive despite the induction of ROS, suggesting that ROS are beneficial for the virus. One canonical role of ROS is to defend the cell against invading bacterial and viral pathogens. Reactive oxygen species (ROS) are by-products of cellular respiration that can promote oxidative stress and damage cellular proteins and lipids.
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