Severe acute respiratory syndrome coronavirus non-structural protein 13 helicase (nsp13)

The Severe acute respiratory syndrome coronavirus non-structural protein 13 (nsp13) is a multi-functional enzyme that plays a critical role in the replication and transcription of the viral genome (UniProt P0C6X7). As a member of the Superfamily 1 (SF1) helicases, it utilizes the energy derived from ATP hydrolysis to unwind double-stranded RNA or DNA in a 5' to 3' direction (Adedeji et al., 2012). Beyond its helicase activity, nsp13 also exhibits NTPase and RNA 5'-triphosphatase activities, the latter being essential for the viral mRNA capping process which facilitates immune evasion and protein synthesis (Ivanov et al., 2004). Due to its high degree of sequence conservation among coronaviruses, nsp13 is considered an attractive target for broad-spectrum antiviral therapy (Shu et al., 2020). Small molecule inhibitors, such as SSYA10-001 and various flavonoids like Myricetin, have been identified to disrupt its enzymatic functions, thereby halting viral replication (Adedeji et al., 2014). The enzyme's unique N-terminal zinc-binding domain and its interaction with the viral polymerase complex (nsp12) further highlight its importance as a therapeutic focal point (Jia et al., 2019).

Other names

nsp13SARS-CoV nsp13Non-structural protein 13SARS-CoV RNA helicaseHelicase/NTPase

Inhibition of ATP-dependent nucleic acid unwinding and NTPase activity