Influenza virus RNA polymerase PB2 subunit (PB2)

The Influenza virus RNA polymerase PB2 subunit is one of the three essential components of the influenza virus RNA-dependent RNA polymerase complex, which is responsible for viral RNA transcription and replication. PB2 binds and recognizes capped host RNA (the "cap-snatching" step) to generate primers for viral mRNA synthesis, with its cap-binding domain playing a critical role in this process[2][3]. The C-terminal domain of PB2, including the lysine 627 residue, is a determinant of pathogenicity and host specificity; mutations at this site can alter the ability of the virus to infect and cause disease in humans and animals[1]. PB2 also interacts with host proteins involved in innate immune signaling, such as the mitochondrial antiviral signaling protein (MAVS), and can modulate the host's antiviral response[4]. PB2 is considered a therapeutic target for antiviral drug development, emphasizing the inhibition of its cap-binding activity and RNA primer recognition functions. Although most established influenza antivirals do not target PB2, several agents in development aim to directly inhibit PB2's functions to counter viral replication and reduce pathogenicity[1].

Other names

PB2Polymerase basic protein 2RNA polymerase PB2 subunitInfluenza polymerase subunit PB2

Experimental drugs targeting PB2 typically inhibit the RNA cap-binding activity or block primer/promoter RNA binding, thereby preventing viral mRNA synthesis and genome replication.