Just how RIG-I signaling is normally regulated, however, hadn't been known.
In the current study, UT Southwestern researchers found that RIG-I and LGP2 each contain a repressor domain, a sort of docking site that controls the actions of each protein. The domain is the key site that regulates the ability of RIG-I to bind to its signaling partners, including LGP2, acting as a switch for controlling immune response, Dr. Gale said.
"Hepatitis C and others viruses hijack this signaling pathway to stop immune defenses," he said.
His research team and others are working to design novel therapeutics and drugs that could mimic viral effects on RIG-I to spur antiviral response or, conversely, mimic viral effects on LGP2 to shut down RIG-I activity. RIG-I shutdown would be necessary in cases when the immune system's response to a virus is dangerously overactive, which happened in many flu cases during the 1918 pandemic.
"Fine-tuning immune response to infection is where antiviral or immune regulatory drugs are headed," said Dr. Gale.
Source:UT Southwestern Medical Center