This is significant because the CARD domain is where two cytosolic proteins bind to activate MAVS, signaling that there is a virus present in the cell.

[7][8][9][10] RIG-I and MDA5 differ in the viral RNA that they recognize, but they share many structural features, including the N-terminal CARD that allows them to bind to MAVS.

[7][8] The formation of this MAVS signaling complex is aided by augmented levels of mitochondrial reactive oxygen species (mROS), independent of the RNA sensing.

MAVS protein induces apoptosis in host virally infected cells by interacting with a protease called caspase 8.

[7] Certain viruses, such as human cytomegalovirus (HCMV) and hepatitis C (HCV), have adapted to suppress the function of MAVS in the antiviral innate immune response, aiding in viral replication.

[7][11] HCMV impairs MAVS through the viral mitochondria-localized inhibitor of apoptosis protein (vMIA), thus reducing the pro-inflammatory cytokine response.

At the transcriptional level, the reactive oxygen species (ROS) generated during antiviral response acts as a negative regulator.