Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of a potentially fatal disease named coronavirus disease 2019 (COVID-19), has raised significant public health concerns globally. To date, the COVID-19 pandemic has caused millions of people to be infected with SARS-CoV-2 worldwide. It has been known since the 2003 SARS epidemic that coronaviruses (CoVs) have large RNA genomes, the replication of which requires an RNA-dependent RNA replication/transcription complex. CoV nonstructural proteins (Nsps) play pivotal roles in the assembly of this complex and associated enzymatic functions in virus genomic replication. Several smaller nonenzymatic Nsps assist with RNA-dependent RNA polymerase function. In this study, we determined the structure of SARS-CoV-2 nonstructural protein 9 (nsp9), an RNA-binding protein that is essential for CoV replication. Its homotetrameric structure with two stable dimeric interfaces provids a structural basis for understanding the mechanisms of RNA-binding protein self-assembly, which may be essential for the regulation of viral RNA replication and transcription.
【저자키워드】 COVID-19, SARS-CoV-2, Nsp9, tetramer, 【초록키워드】 coronavirus disease, public health, COVID-19 pandemic, Transcription, virus, RNA, Replication, Protein, Epidemic, RNA-dependent RNA polymerase, CoV, nonstructural protein, Viral RNA, genomic, mechanism, function, Coronavirus-2, NSP, acute respiratory syndrome, Regulation, complex, CoVs, CoV replication, fatal disease, RNA genomes, caused, raised, 2003 SARS, coronavirus, assist, dimeric, infected with SARS-CoV-2, 【제목키워드】 Protein,