Publication date: Dec 01, 2026
Coronavirus helicase NSP13 is essential for viral replication and transcription and is a promising target for broad-spectrum anti-coronavirus drugs due to its high sequence conservation and structural homology. This review summarizes NSP13 sequence features, structural organization, and functional activities across the seven human-infecting coronaviruses. We outline key enzymatic properties, including duplex RNA/DNA unwinding and NTP hydrolysis, and describe how NSP13 cooperates with other nonstructural proteins to drive replication and transcription. Beyond canonical helicase roles, we discuss the genomic distribution of G-quadruplex (G4) elements in coronaviruses and potential functional connections between G4 structures and NSP13 in regulating the viral life cycle. Finally, we highlight recent progress in developing NSP13-targeting inhibitors and consider their potential utility against COVID-19 and other emerging coronaviruses, providing a rationale for broad-spectrum antiviral design.
Semantics
| Type | Source | Name |
|---|---|---|
| pathway | KEGG | Viral replication |
| pathway | KEGG | Viral life cycle |
| disease | MESH | COVID-19 |