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Regulation of RIG-I activity by phase separation reveals new therapeutic opportunities
After virus infection, RIG-I forms disulfide-linked oligomers that are resistant to degradation and able to enter liquid-like condensates, which is necessary for RIG-I-mediated stimulation of type I interferon signalling. RIG-I agonists and antagonists that enhance or prevent formation of disulfide-linked RIG-I oligomers, respectively, confirm that this mechanism is crucial for RIG-I function and could be harnessed to boost antiviral immunity or suppress autoimmunity caused by hyperactive RIG-I.
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