Innate immunity is a self-defense mechanism that fights against viral and microbial pathogens. This mechanism in our cells uses protein receptors that recognize the general features of pathogens without prior exposure. Upon selective recognition of pathogens, the protein receptors of the innate immunity get activated and stimulate a cascade of signaling events that leads to a rapid immune response against the infection. We are studying the RIG-I (retinoic acid-inducible gene-I) family of innate immunity receptors that detect the most common RNA viruses that infect us, including Influenza, Hepatitis C, Dengue, West Nile, Respiratory Syncytial, Reovirus, and Ebola. The RIG-I family proteins are helicase/ATPase enzymes, and our research aims to understand the mechanism of 'self' versus 'non-self' discrimination by these proteins and the role of helicase/ATPase activity in this process.
 
We are interested in addressing some of these basic questions:

• How do RIG-I receptors distinguish between viral and cellular RNAs?
• What are the atypical RNA features in the viral RNA that are detected by the RIG-I receptors?
• How do these proteins become activated upon binding RNA?
• What is the role of the helicase and ATP hydrolysis activities in the selective recognition of viral RNA?