RNA-dependent RNA polymerase of SARS-CoV-2 (RdRp)

RNA-dependent RNA polymerase of SARS-CoV-2 is an essential viral enzyme responsible for the replication and transcription of the positive-sense RNA genome of the virus[1][2][6]. The core polymerase activity resides in non-structural protein 12 (nsp12), which forms a complex with cofactors nsp7 and nsp8, greatly enhancing activity and processivity[1][2][6]. This polymerase synthesizes new viral RNAs using RNA templates, orchestrating both genome replication and subgenomic transcription necessary for viral gene expression[4]. Its central role in viral propagation makes it a prime therapeutic target—most notably for antiviral drugs such as remdesivir, which mimics nucleotide substrates and terminates RNA chain elongation, thereby suppressing viral replication[2][3]. Structural studies have elucidated the architecture of the RdRp complex and its interaction with inhibitors, providing a foundation for ongoing antiviral drug development[1][2][3][6].

Other names

RNA-dependent RNA polymerase (RdRp)nsp12non-structural protein 12SARS-CoV-2 RdRpcoronavirus polymerase

Inhibition of RNA chain elongation by incorporation of nucleotide analogues (e.g., remdesivir acts as a delayed chain terminator after incorporation into viral RNA); Inducing proofreading errors or mutations in the viral genome; Direct inhibition of catalytic activity of the polymerase complex