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Reactive oxygen species oxidize STING and suppress interferon production
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Journal Article
Reactive oxygen species oxidize STING and suppress interferon production
2020
Overview
Reactive oxygen species (ROS) are by-products of cellular respiration that can promote oxidative stress and damage cellular proteins and lipids. One canonical role of ROS is to defend the cell against invading bacterial and viral pathogens. Curiously, some viruses, including herpesviruses, thrive despite the induction of ROS, suggesting that ROS are beneficial for the virus. However, the underlying mechanisms remain unclear. Here, we found that ROS impaired interferon response during murine herpesvirus infection and that the inhibition occurred downstream of cytoplasmic DNA sensing. 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. This inhibited STING polymerization and activation of downstream signaling events. These data indicate that redox regulation of Cysteine 147 of mouse STING, which is equivalent to Cysteine 148 of human STING, controls interferon production. Together, our findings reveal that ROS orchestrates anti-viral immune responses, which can be exploited by viruses to evade cellular defenses.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications, Ltd,eLife Sciences Publications Ltd
Subject
/ Antiviral Agents - immunology
/ Biological response modifiers
/ Cysteine
/ Cystine
/ Herpesvirus 1, Human - immunology
/ Interferon Type I - immunology
/ Membrane Proteins - antagonists & inhibitors
/ Membrane Proteins - metabolism
/ Mice
/ Microbiology and Infectious Disease
/ Reactive Oxygen Species - immunology
/ Reactive Oxygen Species - metabolism
/ STING
/ Thiols
