Severe acute respiratory syndrome coronavirus 2 helicase (NSP13) (NSP13)

The SARS-CoV-2 helicase, designated as non-structural protein 13 (NSP13), is a critical enzyme for the viral replication-transcription complex (UniProt: P0DTD1). It is a member of the Superfamily 1B (SF1B) helicases and utilizes the energy derived from ATP hydrolysis to unwind double-stranded RNA (dsRNA) or DNA-RNA hybrids in a 5' to 3' direction (PubMed: 32716294). In addition to its helicase function, NSP13 exhibits RNA 5'-triphosphatase activity, which is the first step in the viral mRNA capping process, essential for protecting viral RNA from host cell degradation and ensuring efficient translation (PubMed: 33035244). Due to its high degree of sequence conservation among coronaviruses, NSP13 is an attractive target for broad-spectrum antiviral therapy (PubMed: 34127431). Small molecule inhibitors, such as bismuth-based compounds and certain flavonoids, are being explored to disrupt its enzymatic activities, thereby halting viral proliferation and potentially reducing the severity of COVID-19 (PubMed: 33035244, 32941143).

Other names

Non-structural protein 13SARS-CoV-2 NSP13RNA helicaseNTPase/helicaseReplicase polyprotein 1ab (NSP13 region)

Inhibition of ATP hydrolysis (ATPase activity), inhibition of RNA unwinding activity, and interference with the RNA-binding site to prevent viral replication and transcription.